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Volumn 245, Issue 2, 1997, Pages 355-363

Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes

Author keywords

Alzheimer; Circular dichroism; Peptide lipid interaction; Phosholipid; amyloid peptide

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0030892291     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-2-00355.x     Document Type: Article
Times cited : (181)

References (53)
  • 1
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of β-amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation
    • Aksenov, M. Y., Aksenov, M. V., Butterfield, D. A., Hensley, K., Vigo-Pelfrey, C. & Carney, J. M. (1996) Glutamine synthetase-induced enhancement of β-amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation, J. Neurochem. 66, 2050-2056.
    • (1996) J. Neurochem. , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenov, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 2
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., Rojas, E. & Pollard, H. B. (1993a) Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum, Proc. Natl Acad. Sci. USA 90, 567-571.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 3
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes
    • Arispe, N., Pollard, H. B. & Rojas, E. (1993b) Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes, Proc Natl Acad. Sci. USA 90, 10 573-10 577.
    • (1993) Proc Natl Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 4
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Barlett, G. R. (1959) Phosphorus assay in column chromatography, J. Biol. Chem. 234, 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Barlett, G.R.1
  • 5
    • 0025779179 scopus 로고
    • Structure of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J. & Zagorski, M. G. (1991) Structure of beta peptide and its constituent fragments: relation to amyloid deposition, Science 253, 179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 7
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid beta precursor
    • Cai, X.-D., Golde, T. E. & Younkin, G. S. (1993) Release of excess amyloid beta protein from a mutant amyloid beta precursor, Science 259, 514-516.
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, G.S.3
  • 8
    • 0029379605 scopus 로고
    • Processing of the β-amyloid precursor protein and its regulation in Alzheimer's Disease
    • Checler, F. (1995) Processing of the β-amyloid precursor protein and its regulation in Alzheimer's Disease, J. Neurochem. 65, 1431-1444.
    • (1995) J. Neurochem. , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 9
    • 0028099612 scopus 로고
    • Excessive production of amyloid β-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation
    • Citron, M., Vigo-Pelfrey, C., Teplow, D. B., Miller, C., Schenk, D., Johnston, J., Winblad, B., Venizelos, N., Lannfelt, L. & Selkoe, D. (1994) Excessive production of amyloid β-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation, Proc. Natl Acad. Sci. USA 91, 11 993-11 997.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11993-11997
    • Citron, M.1    Vigo-Pelfrey, C.2    Teplow, D.B.3    Miller, C.4    Schenk, D.5    Johnston, J.6    Winblad, B.7    Venizelos, N.8    Lannfelt, L.9    Selkoe, D.10
  • 10
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey, C. E. (1990) The actions of melittin on membranes, Biochim. Biophys. Acta 1031, 143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 11
    • 0022516431 scopus 로고
    • Morphological changes of phosphatidylcholine bilayers induced by melittin: Vesicularization, fusion, discoidal particles
    • Dufourcq, J., Faucon, J.-F., Fourche, G., Dasseux, J.-L., LeMaire, M. & Gulik-Krzywicki, T. (1986) Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles, Biochim. Biophys. Acta 859, 33-48.
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 33-48
    • Dufourcq, J.1    Faucon, J.-F.2    Fourche, G.3    Dasseux, J.-L.4    LeMaire, M.5    Gulik-Krzywicki, T.6
  • 13
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • Fraser, P. E., Nguyen, J. T., Surewicz, W. K. & Kirschner, D. A. (1991) pH-dependent structural transitions of Alzheimer amyloid peptides, Biophys. J. 60, 1190-1201.
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 14
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser, P. E., Nguyen, J. T., Chin, D. T. & Kirschner, D. A. (1992) Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions, J. Neurochem. 59, 1531-1540.
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 15
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attentuated total reflection infrared study
    • Frey, S. & Tamm, L. K. (1991) Orientation of melittin in phospholipid bilayers. A polarized attentuated total reflection infrared study, Biophys. J. 60, 922-930.
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 16
    • 0030064140 scopus 로고    scopus 로고
    • Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's Disease
    • Fukumoto, H., Asami-Odaka, A., Suzuki, N., Shimada, H., Ihara, Y. & Iwatsubo, T. (1996) Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's Disease, Am. J. Pathol. 148, 259-265.
    • (1996) Am. J. Pathol. , vol.148 , pp. 259-265
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Shimada, H.4    Ihara, Y.5    Iwatsubo, T.6
  • 17
    • 0027218376 scopus 로고
    • Defensins promote fusion and lysis of negatively charged membranes
    • Fujii, G., Selsted, M. E. & Eisenberg, D. (1993) Defensins promote fusion and lysis of negatively charged membranes. Protein Sci. 2, 1301-1312.
    • (1993) Protein Sci. , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 18
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G. & Wong, C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochem. Biophys. Res. Commun. 120, 883-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 883-890
    • Glenner, G.G.1    Wong, C.W.2
  • 19
    • 0028915895 scopus 로고
    • Amyloid β protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms of Aβ40 and Aβ42(43)
    • Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N. & Younkin, S. G. (1995) Amyloid β protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms of Aβ40 and Aβ42(43), J. Biol. Chem. 270, 7013-7016.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3    Long, K.E.4    Otvos, L.5    Younkin, L.H.6    Suzuki, N.7    Younkin, S.G.8
  • 21
    • 0013795179 scopus 로고
    • Stabilities of metal complexes of phospholipids: Ca(II), Mg(II) and Ni(II) complexes of phosphatylserine and triphosphinositide
    • Hendrickson, H. S. & Fullington, J. G. (1965) Stabilities of metal complexes of phospholipids: Ca(II), Mg(II) and Ni(II) complexes of phosphatylserine and triphosphinositide, Biochemistry 4, 1599.
    • (1965) Biochemistry , vol.4 , pp. 1599
    • Hendrickson, H.S.1    Fullington, J.G.2
  • 22
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C. L. & Beyreuther, K. (1991) Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease, J. Mol. Biol. 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    Beyreuther, K.5
  • 23
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N. & Ihara, Y. (1994) Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43), Neuron 13, 45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 24
    • 0028919919 scopus 로고
    • Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down Syndrome
    • Iwatsubo, T., Mann, D. M., Odaka, A., Suzuki, N. & Ihara, Y. (1995) Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down Syndrome, Ann. Neurol. 37, 294-299.
    • (1995) Ann. Neurol. , vol.37 , pp. 294-299
    • Iwatsubo, T.1    Mann, D.M.2    Odaka, A.3    Suzuki, N.4    Ihara, Y.5
  • 25
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and Scrapie?
    • Jarrett, J. T. & Lansbury, P. T. (1993) Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and Scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 26
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T., Berger, E. P. & Lanbury, P. T. (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease, Biochemistry 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lanbury, P.T.3
  • 27
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., Selsted, M. E., Ganz, T. & Lehrer, R. I. (1990) Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes, Proc. Natl Acad. Sci. USA 87, 210-214.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 28
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer's Disease indicates cross-β conformation
    • Kirschner D. A., Abraham, C. & Selkoe, D. J. (1986) X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer's Disease indicates cross-β conformation, Proc. Natl Acad. Sci. USA 83, 503-507.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 29
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomatin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A. & Teplow, D. B. (1996) On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants, Proc. Natl Acad. Sci. USA 93, 1125-1129.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomatin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 30
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo, A. & Yankner, B. (1994) β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red, Proc. Natl Acad. Sci. USA 91, 12243-12247.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.2
  • 31
    • 0029878108 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis
    • Mason, R. P., Estermeyer, J. D., Kelly, J. F. & Mason, P. E. (1996) Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis, Biochem. Biophys. Res. Commun. 222, 78-82.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 78-82
    • Mason, R.P.1    Estermeyer, J.D.2    Kelly, J.F.3    Mason, P.E.4
  • 32
    • 0029861772 scopus 로고    scopus 로고
    • Membrane disruption by Alzheimer β-amyloid peptides mediated by specific binding to either phospholipids or gangliosides: Implications for neurotoxicity
    • McLaurin, J. & Chakrabartty, A. (1996) Membrane disruption by Alzheimer β-amyloid peptides mediated by specific binding to either phospholipids or gangliosides: implications for neurotoxicity, J. Biol. Chem. 271, 26482-26489.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26482-26489
    • McLaurin, J.1    Chakrabartty, A.2
  • 34
    • 0028804445 scopus 로고
    • Modulation of mellittin-induced lysis by surface charge density of membranes
    • Monette, M. & Lafleur, M. (1995) Modulation of mellittin-induced lysis by surface charge density of membranes, Biophys. J. 68, 187-195.
    • (1995) Biophys. J. , vol.68 , pp. 187-195
    • Monette, M.1    Lafleur, M.2
  • 36
    • 0027981038 scopus 로고
    • Interaction of melittin with lipid membranes, Biochim
    • Ohki, S., Marcus, E., Sukumaran, D. K. & Arnold, K. (1994) Interaction of melittin with lipid membranes, Biochim. Biophys. Acta 1194, 223-232.
    • (1994) Biophys. Acta , vol.1194 , pp. 223-232
    • Ohki, S.1    Marcus, E.2    Sukumaran, D.K.3    Arnold, K.4
  • 37
    • 0025253204 scopus 로고
    • Design and synthesis of basic peptides having amphipathic β-structure and their interaction with phospholipid membranes
    • Ono, S., Lee, S., Mihara, H., Aoyagi, H., Kato, T. & Yamasaki, N. (1990) Design and synthesis of basic peptides having amphipathic β-structure and their interaction with phospholipid membranes, Biochim. Biophys. Acta 1022, 237-244.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 237-244
    • Ono, S.1    Lee, S.2    Mihara, H.3    Aoyagi, H.4    Kato, T.5    Yamasaki, N.6
  • 38
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G. & Cotman, C. W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state, J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 39
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue
    • Roher, A. E., Palmer, K. C., Surewicz, E. C., Ball, M. J. & Greenberg, B. D. (1993) Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue, J. Neurochem. 61, 1916-1926.
    • (1993) J. Neurochem. , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Surewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 40
    • 0028147455 scopus 로고
    • Fragmentation of phospholipid bilayers by myelin basic protein
    • Roux, M., Nezil, F. A., Monck, M. & Bloom, M. (1994) Fragmentation of phospholipid bilayers by myelin basic protein, Biochemistry 33, 307-311.
    • (1994) Biochemistry , vol.33 , pp. 307-311
    • Roux, M.1    Nezil, F.A.2    Monck, M.3    Bloom, M.4
  • 41
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. (1991) The molecular pathology of Alzheimer's disease, Neuron 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 43
    • 0024273721 scopus 로고
    • The presence of heparan sulfate proteoglycans in neuritic plaques and congophilic angiopathy in Alzheimer's Disease
    • Snow, A. D., Mar, H., Nochlin, D., Kimata, K., Kato, M., Suzuki, S., Hassell, J. & Wight, T. N. (1988) The presence of heparan sulfate proteoglycans in neuritic plaques and congophilic angiopathy in Alzheimer's Disease, Am. J. Pathol. 133, 456-463.
    • (1988) Am. J. Pathol. , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimata, K.4    Kato, M.5    Suzuki, S.6    Hassell, J.7    Wight, T.N.8
  • 44
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow, A. D., Mar, H., Nochlin, D., Kresse, H. & Wight, T. N. (1992) Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease, J. Histochem. Cytochem. 40, 105-113.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 45
    • 0027479901 scopus 로고
    • Interaction of myelin basic-protein with artificial membranes. Parameters governing binding, aggregation and dissociation
    • ter Beest, M. B. A. & Hoekstra, D. (1993) Interaction of myelin basic-protein with artificial membranes. Parameters governing binding, aggregation and dissociation, Eur. J. Biochem. 211, 689-696.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 689-696
    • Ter Beest, M.B.A.1    Hoekstra, D.2
  • 46
    • 0028179865 scopus 로고
    • Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi, E., Holzemann, G. & Seelig, J. (1994) Alzheimer β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes. Biochemistry 33, 7434-7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 47
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi, E., Holzemann, G. & Seelig, J. (1995) Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes, J. Mol. Biol. 252, 633-642.
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 49
  • 50
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: Structural and thermodynamic basis for partitioning and folding
    • White, S. H. & Wimley, W. C. (1994) Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding, Curr. Opin. Struct. Biol. 4, 79-86.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 79-86
    • White, S.H.1    Wimley, W.C.2
  • 51
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., Wimley, W. C. & Selsted, M. E. (1995) Structure, function, and membrane integration of defensins, Curr. Opin. Struct. Biol. 5, 521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 52
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., Selsted, M. E. & White, S. H. (1994) Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores, Protein Sci. 3, 1362-1373.
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 53
    • 0024339121 scopus 로고
    • The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carinoma-associated amyloidosis
    • Young, I. D., Willmer, J. P. & Kisilevsky, R. (1989) The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carinoma-associated amyloidosis, Acta Neuropathol. 78, 202-209.
    • (1989) Acta Neuropathol. , vol.78 , pp. 202-209
    • Young, I.D.1    Willmer, J.P.2    Kisilevsky, R.3


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