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Volumn 371, Issue 4, 2007, Pages 924-933

Formation of Amyloids by Aβ-(1-42) on NGF-differentiated PC12 Cells: Roles of Gangliosides and Cholesterol

Author keywords

amyloid protein; cholesterol; gangliosides; NGF differentiation; visualization

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN[1-42]; CHOLESTEROL; COMPACTIN; CONGO RED; GANGLIOSIDE; NERVE GROWTH FACTOR; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; UNCLASSIFIED DRUG;

EID: 34547118151     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.008     Document Type: Article
Times cited : (69)

References (62)
  • 1
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe D.J. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10 (1994) 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 J.D., and Lansbury Jr. P.T. 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. 66 (1997) 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 Jr. P.T. Structural neurology: are seeds at the root of neuronal degeneration?. Neuron 19 (1997) 1151-1154
    • (1997) Neuron , vol.19 , pp. 1151-1154
    • Lansbury Jr., P.T.1
  • 4
    • 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., and Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nature Med. 1 (1995) 1062-1066
    • (1995) Nature Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 5
    • 0031957080 scopus 로고    scopus 로고
    • GM1 ganglioside-bound amyloid β-protein in Alzheimer's disease brain
    • Yanagisawa K., and Ihara Y. GM1 ganglioside-bound amyloid β-protein in Alzheimer's disease brain. Neurobiol. Aging 19 (1998) S65-S67
    • (1998) Neurobiol. Aging , vol.19
    • Yanagisawa, K.1    Ihara, Y.2
  • 7
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells
    • Morishima-Kawashima M., and Ihara Y. The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells. Biochemistry 37 (1998) 15247-15253
    • (1998) Biochemistry , vol.37 , pp. 15247-15253
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 8
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 9
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric amyloid β protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease
    • Kawarabayashi T., Shoji M., Younkin L.H., Wen-Lang L., Dickson D.W., Murakami T., et al. Dimeric amyloid β protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease. J. Neurosci. 24 (2004) 3801-3809
    • (2004) J. Neurosci. , vol.24 , pp. 3801-3809
    • Kawarabayashi, T.1    Shoji, M.2    Younkin, L.H.3    Wen-Lang, L.4    Dickson, D.W.5    Murakami, T.6
  • 10
    • 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.I., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276 (2001) 24985-24990
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.I.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 11
    • 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., and 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 41 (2002) 7385-7390
    • (2002) Biochemistry , vol.41 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 12
    • 34547350809 scopus 로고    scopus 로고
    • Matsuzaki, K. (2007). Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim. Biophys. Acta, In the press.
  • 14
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist M., Lindström F., Watts A., and Gröbner G. Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335 (2004) 1039-1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindström, F.2    Watts, A.3    Gröbner, G.4
  • 17
    • 33750475909 scopus 로고    scopus 로고
    • Fucosyl-GM1 expression and amyloid-β protein accumulation in PC12 cells
    • Yanagisawa M., Ariga T., and Yu R.K. Fucosyl-GM1 expression and amyloid-β protein accumulation in PC12 cells. J. Neurosci. Res. 84 (2006) 1343-1349
    • (2006) J. Neurosci. Res. , vol.84 , pp. 1343-1349
    • Yanagisawa, M.1    Ariga, T.2    Yu, R.K.3
  • 18
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid β-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • Van Nostrand W.E., Melchor J.P., and Ruffini L. Pathologic amyloid β-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J. Neurochem. 70 (1998) 216-223
    • (1998) J. Neurochem. , vol.70 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3
  • 19
    • 28244452110 scopus 로고    scopus 로고
    • Cross-seeding of wild-type and hereditary variant-type amyloid β-proteins in the presence of gangliosides
    • Yamamoto N., Matsuzaki K., and Yanagisawa K. Cross-seeding of wild-type and hereditary variant-type amyloid β-proteins in the presence of gangliosides. J. Neurochem. 95 (2005) 1167-1176
    • (2005) J. Neurochem. , vol.95 , pp. 1167-1176
    • Yamamoto, N.1    Matsuzaki, K.2    Yanagisawa, K.3
  • 20
    • 34047269583 scopus 로고    scopus 로고
    • GM1-ganglioside-induced Aβ assembly on synaptic membranes of cultured neurons
    • Yamamoto N., Fukata Y., Fukata M., and Yanagisawa K. GM1-ganglioside-induced Aβ assembly on synaptic membranes of cultured neurons. Biochim. Biophys. Acta 1768 (2007) 1128-1137
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1128-1137
    • Yamamoto, N.1    Fukata, Y.2    Fukata, M.3    Yanagisawa, K.4
  • 21
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A re-evaluation of the mechanism of cellular uptake
    • Richard J.P., Melikov K., Vives E., Ramos C., Verbeure B., Gait M.J., et al. Cell-penetrating peptides. A re-evaluation of the mechanism of cellular uptake. J. Biol. Chem. 278 (2003) 585-590
    • (2003) J. Biol. Chem. , vol.278 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Vives, E.3    Ramos, C.4    Verbeure, B.5    Gait, M.J.6
  • 22
    • 0035834692 scopus 로고    scopus 로고
    • Reduction in cholesterol and sialic acid content protects cells from the toxic effects of β-amyloid peptides
    • Wang S.S., Rymer D.L., and Good T.A. Reduction in cholesterol and sialic acid content protects cells from the toxic effects of β-amyloid peptides. J. Biol. Chem. 276 (2001) 42027-42034
    • (2001) J. Biol. Chem. , vol.276 , pp. 42027-42034
    • Wang, S.S.1    Rymer, D.L.2    Good, T.A.3
  • 24
    • 2542493177 scopus 로고    scopus 로고
    • Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol
    • Sato S.B., Ishii K., Makino A., Iwabuchi K., Yamaji-Hasegawa A., Senoh Y., et al. Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol. J. Biol. Chem. 279 (2004) 23790-23796
    • (2004) J. Biol. Chem. , vol.279 , pp. 23790-23796
    • Sato, S.B.1    Ishii, K.2    Makino, A.3    Iwabuchi, K.4    Yamaji-Hasegawa, A.5    Senoh, Y.6
  • 25
    • 21244492425 scopus 로고    scopus 로고
    • Delineation of positron emission tomography imaging agent binding sites on β-amyloid peptide fibrils
    • Ye L., Morgenstern J.L., Gee A.D., Hong G., Brown J., and Lockhart A. Delineation of positron emission tomography imaging agent binding sites on β-amyloid peptide fibrils. J. Biol. Chem. 280 (2005) 23599-23604
    • (2005) J. Biol. Chem. , vol.280 , pp. 23599-23604
    • Ye, L.1    Morgenstern, J.L.2    Gee, A.D.3    Hong, G.4    Brown, J.5    Lockhart, A.6
  • 27
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H., Tuominen E.K., and Kinnunen P.K. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 (2004) 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.2    Kinnunen, P.K.3
  • 28
    • 7544245555 scopus 로고    scopus 로고
    • Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers
    • Sparr E., Engel M.F., Sakharov D.V., Sprong M., Jacobs J., de Kruijff B., et al. Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. FEBS Letters 577 (2004) 117-120
    • (2004) FEBS Letters , vol.577 , pp. 117-120
    • Sparr, E.1    Engel, M.F.2    Sakharov, D.V.3    Sprong, M.4    Jacobs, J.5    de Kruijff, B.6
  • 29
    • 4043164892 scopus 로고    scopus 로고
    • Overexpressed GM1 suppresses nerve growth factor (NGF) signals by modulating the intracellular localization of NGF receptors and membrane fluidity in PC12 cells
    • Nishio M., Fukumoto S., Furukawa K., Ichimura A., Miyazaki H., Kusunoki S., et al. Overexpressed GM1 suppresses nerve growth factor (NGF) signals by modulating the intracellular localization of NGF receptors and membrane fluidity in PC12 cells. J. Biol. Chem. 279 (2004) 33368-33378
    • (2004) J. Biol. Chem. , vol.279 , pp. 33368-33378
    • Nishio, M.1    Fukumoto, S.2    Furukawa, K.3    Ichimura, A.4    Miyazaki, H.5    Kusunoki, S.6
  • 30
    • 0032433258 scopus 로고    scopus 로고
    • β-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis
    • Ivins K.J., Bui E.T., and Cotman C.W. β-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis. Neurobiol. Dis. 5 (1998) 365-378
    • (1998) Neurobiol. Dis. , vol.5 , pp. 365-378
    • Ivins, K.J.1    Bui, E.T.2    Cotman, C.W.3
  • 31
    • 33746214688 scopus 로고    scopus 로고
    • Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to Aβ in distal axons
    • Song M.S., Saavedra L., and de Chaves E.I. Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to Aβ in distal axons. Neurobiol. Aging 27 (2006) 1224-1238
    • (2006) Neurobiol. Aging , vol.27 , pp. 1224-1238
    • Song, M.S.1    Saavedra, L.2    de Chaves, E.I.3
  • 32
    • 33751221596 scopus 로고    scopus 로고
    • Increased cholesterol in Aβ-positive nerve terminals from Alzheimer's disease cortex
    • Gylys K.H., Fein J.A., Yang F., Miller C.A., and Cole G.M. Increased cholesterol in Aβ-positive nerve terminals from Alzheimer's disease cortex. Neurobiol. Aging 28 (2007) 8-17
    • (2007) Neurobiol. Aging , vol.28 , pp. 8-17
    • Gylys, K.H.1    Fein, J.A.2    Yang, F.3    Miller, C.A.4    Cole, G.M.5
  • 33
    • 33745052350 scopus 로고    scopus 로고
    • Cyclodextrins but not compactin inhibit the lateral diffusion of membrane proteins independent of cholesterol
    • Shvartsman D.E., Gutman O., Tietz A., and Henis Y.I. Cyclodextrins but not compactin inhibit the lateral diffusion of membrane proteins independent of cholesterol. Traffic 7 (2006) 917-926
    • (2006) Traffic , vol.7 , pp. 917-926
    • Shvartsman, D.E.1    Gutman, O.2    Tietz, A.3    Henis, Y.I.4
  • 34
    • 0033922431 scopus 로고    scopus 로고
    • Lipid trafficking and sorting: how cholesterol is filling gaps
    • Hoekstra D., and van I.S.C. Lipid trafficking and sorting: how cholesterol is filling gaps. Curr. Opin. Cell Biol. 12 (2000) 496-502
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 496-502
    • Hoekstra, D.1    van, I.S.C.2
  • 35
    • 0035826795 scopus 로고    scopus 로고
    • A fluid connection: cholesterol and Aβ
    • Wolozin B. A fluid connection: cholesterol and Aβ. Proc. Natl Acad. Sci. USA 98 (2001) 5371-5373
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5371-5373
    • Wolozin, B.1
  • 36
    • 12444340438 scopus 로고    scopus 로고
    • Mild hypercholesterolemia is an early risk factor for the development of Alzheimer amyloid pathology
    • Pappolla M.A., Bryant-Thomas T.K., Herbert D., Pacheco J., Fabra Garcia M., Manjon M., et al. Mild hypercholesterolemia is an early risk factor for the development of Alzheimer amyloid pathology. Neurology 61 (2003) 199-205
    • (2003) Neurology , vol.61 , pp. 199-205
    • Pappolla, M.A.1    Bryant-Thomas, T.K.2    Herbert, D.3    Pacheco, J.4    Fabra Garcia, M.5    Manjon, M.6
  • 38
    • 0001504829 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ 42 and Aβ 40 in vitro and in vivo
    • Fassbender K., Simons M., Bergmann C., Stroick M., Lütjohann D., Keller P., et al. Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ 42 and Aβ 40 in vitro and in vivo. Proc. Natl Acad. Sci. USA 98 (2001) 5856-5861
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5856-5861
    • Fassbender, K.1    Simons, M.2    Bergmann, C.3    Stroick, M.4    Lütjohann, D.5    Keller, P.6
  • 39
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • Ehehalt R., Keller P., Haass C., Thiele C., and Simons K. Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 160 (2003) 113-123
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 40
    • 0029827792 scopus 로고    scopus 로고
    • Cholesterol protects PC12 cells from β-amyloid induced calcium disordering and cytotoxicity
    • Zhou Y., and Richardson J.S. Cholesterol protects PC12 cells from β-amyloid induced calcium disordering and cytotoxicity. Neuroreport 7 (1996) 2487-2490
    • (1996) Neuroreport , vol.7 , pp. 2487-2490
    • Zhou, Y.1    Richardson, J.S.2
  • 41
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara M., Kuroda Y., Arispe N., and Rojas E. Alzheimer's β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J. Biol. Chem. 275 (2000) 14077-14083
    • (2000) J. Biol. Chem. , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 42
    • 0036793543 scopus 로고    scopus 로고
    • Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides
    • Arispe N., and Doh M. Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides. FASEB J. 16 (2002) 1526-1536
    • (2002) FASEB J. , vol.16 , pp. 1526-1536
    • Arispe, N.1    Doh, M.2
  • 43
    • 4644309414 scopus 로고    scopus 로고
    • Membrane cholesterol interferes with neuronal apoptosis induced by soluble oligomers but not fibrils of amyloid-β peptide
    • Sponne I., Fifre A., Koziel V., Oster T., Olivier J.L., and Pillot T. Membrane cholesterol interferes with neuronal apoptosis induced by soluble oligomers but not fibrils of amyloid-β peptide. FASEB J. 18 (2004) 836-838
    • (2004) FASEB J. , vol.18 , pp. 836-838
    • Sponne, I.1    Fifre, A.2    Koziel, V.3    Oster, T.4    Olivier, J.L.5    Pillot, T.6
  • 44
    • 0033532236 scopus 로고    scopus 로고
    • Enhancement of MTT, a tetrazolium salt, exocytosis by amyloid β-protein and chloroquine in cultured rat astrocytes
    • Isobe I., Michikawa M., and Yanagisawa K. Enhancement of MTT, a tetrazolium salt, exocytosis by amyloid β-protein and chloroquine in cultured rat astrocytes. Neurosci. Letters 266 (1999) 129-132
    • (1999) Neurosci. Letters , vol.266 , pp. 129-132
    • Isobe, I.1    Michikawa, M.2    Yanagisawa, K.3
  • 46
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 48
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., et al. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 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
  • 50
    • 34047249085 scopus 로고    scopus 로고
    • A ganglioside-induced toxic soluble Aβ assembly. Its enhanced formation from Aβ bearing the Arctic mutation
    • Yamamoto N., Matsubara E., Maeda S., Minagawa H., Takashima A., Maruyama W., et al. A ganglioside-induced toxic soluble Aβ assembly. Its enhanced formation from Aβ bearing the Arctic mutation. J. Biol. Chem. 282 (2007) 2646-2655
    • (2007) J. Biol. Chem. , vol.282 , pp. 2646-2655
    • Yamamoto, N.1    Matsubara, E.2    Maeda, S.3    Minagawa, H.4    Takashima, A.5    Maruyama, W.6
  • 52
    • 33846813665 scopus 로고    scopus 로고
    • Docosahexaenoic acid stabilizes soluble amyloid-β protofibrils and sustains amyloid-β-induced neurotoxicity in vitro
    • Johansson A.S., Garlind A., Berglind-Dehlin F., Karlsson G., Edwards K., Gellerfors P., et al. Docosahexaenoic acid stabilizes soluble amyloid-β protofibrils and sustains amyloid-β-induced neurotoxicity in vitro. FEBS J. 274 (2007) 990-1000
    • (2007) FEBS J. , vol.274 , pp. 990-1000
    • Johansson, A.S.1    Garlind, A.2    Berglind-Dehlin, F.3    Karlsson, G.4    Edwards, K.5    Gellerfors, P.6
  • 53
    • 34247639567 scopus 로고    scopus 로고
    • Various dendritic abnormalities are associated with fibrillar amyloid deposits in Alzheimer's disease
    • Grutzendler J., Helmin K., Tsai J., and Gan W.B. Various dendritic abnormalities are associated with fibrillar amyloid deposits in Alzheimer's disease. Ann. NY Acad. Sci. 1097 (2007) 30-39
    • (2007) Ann. NY Acad. Sci. , vol.1097 , pp. 30-39
    • Grutzendler, J.1    Helmin, K.2    Tsai, J.3    Gan, W.B.4
  • 54
    • 7044220336 scopus 로고    scopus 로고
    • Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
    • Tsai J., Grutzendler J., Duff K., and Gan W.B. Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nature Neurosci. 7 (2004) 1181-1183
    • (2004) Nature Neurosci. , vol.7 , pp. 1181-1183
    • Tsai, J.1    Grutzendler, J.2    Duff, K.3    Gan, W.B.4
  • 55
    • 0029964207 scopus 로고    scopus 로고
    • Amyloid fibril toxicity in Alzheimer's disease and diabetes
    • Lorenzo A., and Yankner B.A. Amyloid fibril toxicity in Alzheimer's disease and diabetes. Ann. NY Acad. Sci. 777 (1996) 89-95
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 89-95
    • Lorenzo, A.1    Yankner, B.A.2
  • 56
    • 10944272619 scopus 로고    scopus 로고
    • Fibrillar amyloid-β peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease
    • Jana A., and Pahan K. Fibrillar amyloid-β peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease. J. Biol. Chem. 279 (2004) 51451-51459
    • (2004) J. Biol. Chem. , vol.279 , pp. 51451-51459
    • Jana, A.1    Pahan, K.2
  • 57
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307 (2005) 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 58
    • 34447255463 scopus 로고    scopus 로고
    • Okada, T., Wakabayashi, M., Ikeda, K. & Matsuzaki, K. (2007). Formation of toxic fibrils of Alzheimer's amyloid β-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component. J. Mol. Biol. In press.
  • 59
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid β peptide1-42 through p53 and Bax in cultured primary human neurons
    • Zhang Y., McLaughlin R., Goodyer C., and LeBlanc A. Selective cytotoxicity of intracellular amyloid β peptide1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156 (2002) 519-529
    • (2002) J. Cell Biol. , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 60
    • 33845424356 scopus 로고    scopus 로고
    • Inhibitors of amyloid β-protein aggregation mediated by GM1-containing raft-like membranes
    • Matsuzaki K., Noguch T., Wakabayashi M., Ikeda K., Okada T., Ohashi Y., et al. Inhibitors of amyloid β-protein aggregation mediated by GM1-containing raft-like membranes. Biochim. Biophys. Acta 1768 (2007) 122-130
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 122-130
    • Matsuzaki, K.1    Noguch, T.2    Wakabayashi, M.3    Ikeda, K.4    Okada, T.5    Ohashi, Y.6
  • 61
    • 0033598697 scopus 로고    scopus 로고
    • Interaction 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., and Naiki H. Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 38 (1999) 15514-15521
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5
  • 62
    • 21244442348 scopus 로고    scopus 로고
    • Spatial and functional heterogeneity of sphingolipid-rich membrane domains
    • Kiyokawa E., Baba T., Otsuka N., Makino A., Ohno S., and Kobayashi T. Spatial and functional heterogeneity of sphingolipid-rich membrane domains. J. Biol. Chem. 280 (2005) 24072-24084
    • (2005) J. Biol. Chem. , vol.280 , pp. 24072-24084
    • Kiyokawa, E.1    Baba, T.2    Otsuka, N.3    Makino, A.4    Ohno, S.5    Kobayashi, T.6


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