메뉴 건너뛰기




Volumn 53, Issue 48, 2014, Pages 7523-7530

Comparison between the aggregation of human and rodent amyloid β-proteins in GM1 ganglioside clusters

Author keywords

[No Author keywords available]

Indexed keywords

AZO DYES; CYTOLOGY; DEPOSITION; GLYCOPROTEINS; MAMMALS; NEURODEGENERATIVE DISEASES; PATHOLOGY;

EID: 84916219015     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501239q     Document Type: Article
Times cited : (26)

References (57)
  • 1
    • 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. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer' s disease
    • Walsh, D. M., and Selkoe, D. J. (2004) Deciphering the molecular basis of memory failure in Alzheimer' s disease. Neuron 44, 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease
    • Masters, C. L., and Selkoe, D. J. (2012) Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease. Cold Spring Harbor Perspect. Med. 2, a006262.
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. a006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 4
    • 80052501210 scopus 로고    scopus 로고
    • Resolving controversies on the path to Alzheimer's therapeutics
    • Selkoe, D. J. (2011) Resolving controversies on the path to Alzheimer's therapeutics. Nat. Med. 17, 1060-1065.
    • (2011) Nat. Med. , vol.17 , pp. 1060-1065
    • Selkoe, D.J.1
  • 5
    • 0024556348 scopus 로고
    • Biochemistry of altered brain proteins in Alzheimer's disease
    • Selkoe, D. J. (1989) Biochemistry of altered brain proteins in Alzheimer's disease. Annu. Rev. Neurosci. 12, 463-490.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 463-490
    • Selkoe, D.J.1
  • 6
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer 's disease
    • Bush, A. I. (2003) The metallobiology of Alzheimer 's disease. Trends Neurosci. 26, 207-214.
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 9
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease
    • Liu, S. T., Howlett, G., and Barrow, C. J. (1999) Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease. Biochemistry 38, 9373-9378.
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 11
    • 34547350809 scopus 로고    scopus 로고
    • Physicochemical interactions of amyloid β-peptide with lipid bilayers
    • Matsuzaki, K. (2007) Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim. Biophys. Acta 1768, 1935-1942.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1935-1942
    • Matsuzaki, K.1
  • 12
    • 77953235479 scopus 로고    scopus 로고
    • Aβ polymerization through interaction with membrane gangliosides
    • Matsuzaki, K., Kato, K., and Yanagisawa, K. (2010) Aβ polymerization through interaction with membrane gangliosides. Biochim. Biophys. Acta 1801, 868-877.
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 868-877
    • Matsuzaki, K.1    Kato, K.2    Yanagisawa, K.3
  • 13
    • 79952136169 scopus 로고    scopus 로고
    • Formation of toxic amyloid fibrils by amyloid β-protein on ganglioside clusters
    • Matsuzaki, K. (2011) Formation of toxic amyloid fibrils by amyloid β-protein on ganglioside clusters. International Journal of Alzheimer' s Research 2011, ID 956104.
    • (2011) International Journal of Alzheimer' S Research , vol.2011
    • Matsuzaki, K.1
  • 14
    • 84906239240 scopus 로고    scopus 로고
    • How do membranes initiate Alzheimer's disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters
    • Matsuzaki, K. (2014) How do membranes initiate Alzheimer's disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters. Acc. Chem. Res. 47, 2397-2404.
    • (2014) Acc. Chem. Res. , vol.47 , pp. 2397-2404
    • Matsuzaki, K.1
  • 15
    • 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. (1995) GM1 ganglioside-bound amyloid β-protein (Aβ): A possible form of preamyloid in Alzheimer's disease. Nat. Med. 1, 1062-1066.
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 16
    • 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., and Matsuzaki, K. (2001) Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276, 24985-24990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 17
    • 79960506176 scopus 로고    scopus 로고
    • Mechanism of amyloid β-protein aggregation mediated by GM1 ganglioside clusters
    • Ikeda, K., Yamaguchi, T., Fukunaga, S., Hoshino, M., and Matsuzaki, K. (2011) Mechanism of amyloid β-protein aggregation mediated by GM1 ganglioside clusters. Biochemistry 50, 6433-6440.
    • (2011) Biochemistry , vol.50 , pp. 6433-6440
    • Ikeda, K.1    Yamaguchi, T.2    Fukunaga, S.3    Hoshino, M.4    Matsuzaki, K.5
  • 18
    • 51249115821 scopus 로고    scopus 로고
    • Formation of toxic Aβ (1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in Aβ (1-40) fibrils
    • Okada, T., Ikeda, K., Wakabayashi, M., Ogawa, M., and Matsuzaki, K. (2008) Formation of toxic Aβ (1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in Aβ (1-40) fibrils. J. Mol. Biol. 382, 1066-1074.
    • (2008) J. Mol. Biol. , vol.382 , pp. 1066-1074
    • Okada, T.1    Ikeda, K.2    Wakabayashi, M.3    Ogawa, M.4    Matsuzaki, K.5
  • 19
    • 84867533254 scopus 로고    scopus 로고
    • GM1 cluster mediates formation of toxic Aβ fibrils by providing hydrophobic environments
    • Fukunaga, S., Ueno, H., Yamaguchi, T., Yano, Y., Hoshino, M., and Matsuzaki, K. (2012) GM1 cluster mediates formation of toxic Aβ fibrils by providing hydrophobic environments. Biochemistry 51, 8125-8131.
    • (2012) Biochemistry , vol.51 , pp. 8125-8131
    • Fukunaga, S.1    Ueno, H.2    Yamaguchi, T.3    Yano, Y.4    Hoshino, M.5    Matsuzaki, K.6
  • 20
    • 13844256497 scopus 로고    scopus 로고
    • Production of recombinant amyloid-β peptide 42 as an ubiquitin extension
    • Lee, E. K., Hwang, J. H., Shin, D. Y., Kim, D. I., and Yoo, Y. J. (2005) Production of recombinant amyloid-β peptide 42 as an ubiquitin extension. Protein Expression Purif. 40, 183-189.
    • (2005) Protein Expression Purif. , vol.40 , pp. 183-189
    • Lee, E.K.1    Hwang, J.H.2    Shin, D.Y.3    Kim, D.I.4    Yoo, Y.J.5
  • 21
    • 77955680341 scopus 로고    scopus 로고
    • A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation
    • Yamaguchi, T., Yagi, H., Goto, Y., Matsuzaki, K., and Hoshino, M. (2010) A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation. Biochemistry 49, 7100-7107.
    • (2010) Biochemistry , vol.49 , pp. 7100-7107
    • Yamaguchi, T.1    Yagi, H.2    Goto, Y.3    Matsuzaki, K.4    Hoshino, M.5
  • 22
    • 34447255463 scopus 로고    scopus 로고
    • Formation of toxic fibrils of Alzheimer's amyloid β-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component
    • Okada, T., Wakabayashi, M., Ikeda, K., and 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. 371, 481-489.
    • (2007) J. Mol. Biol. , vol.371 , pp. 481-489
    • Okada, T.1    Wakabayashi, M.2    Ikeda, K.3    Matsuzaki, K.4
  • 23
    • 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. (2005) Cross-seeding of wild-type and hereditary variant type amyloid β-proteins in the presence of gangliosides. J. Neurochem. 95, 1167-1176.
    • (2005) J. Neurochem. , vol.95 , pp. 1167-1176
    • Yamamoto, N.1    Matsuzaki, K.2    Yanagisawa, K.3
  • 24
    • 49749155713 scopus 로고
    • Quantitative estimation of sialic acids. II. A colorimetric resorcinol-hydrochloric acid method
    • Svennerholm, L. (1957) Quantitative estimation of sialic acids. II. A colorimetric resorcinol-hydrochloric acid method. Biochim. Biophys. Acta 24, 604-611.
    • (1957) Biochim. Biophys. Acta , vol.24 , pp. 604-611
    • Svennerholm, L.1
  • 25
    • 79851481547 scopus 로고    scopus 로고
    • Ganglioside-mediated aggregation of amyloid β-proteins (Aβ): Comparison between Aβ-(1-42) and Aβ-(1-40)
    • Ogawa, M., Tsukuda, M., Yamaguchi, T., Ikeda, K., Okada, T., Yano, Y., Hoshino, M., and Matsuzaki, K. (2011) Ganglioside-mediated aggregation of amyloid β-proteins (Aβ): Comparison between Aβ-(1-42) and Aβ-(1-40). J. Neurochem. 116, 851-857.
    • (2011) J. Neurochem. , vol.116 , pp. 851-857
    • Ogawa, M.1    Tsukuda, M.2    Yamaguchi, T.3    Ikeda, K.4    Okada, T.5    Yano, Y.6    Hoshino, M.7    Matsuzaki, K.8
  • 26
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., III (1993) Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2, 404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 27
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • Naiki, H., and Gejyo, F. (1999) Kinetic analysis of amyloid fibril formation. Methods Enzymol. 309, 305-318.
    • (1999) Methods Enzymol. , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 28
    • 0000757008 scopus 로고
    • The conformation of dynorphin A-(1-13) in aqueous solution as studied by Fourier transform infrared spectroscopy
    • Surewicz, W. K., and Mantsch, H. H. (1989) The conformation of dynorphin A-(1-13) in aqueous solution as studied by Fourier transform infrared spectroscopy. J. Mol. Struct. 214, 143-147.
    • (1989) J. Mol. Struct. , vol.214 , pp. 143-147
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 29
    • 4243898367 scopus 로고
    • Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations
    • Miyazawa, T. (1960) Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations. J. Chem. Phys. 32, 1647-1652.
    • (1960) J. Chem. Phys. , vol.32 , pp. 1647-1652
    • Miyazawa, T.1
  • 30
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and II bands
    • Miyazawa, T., and Blout, E. R. (1961) The infrared spectra of polypeptides in various conformations: Amide I and II bands. J. Am. Chem. Soc. 83, 712-719.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 31
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 32
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel β-helix proteins have a unique Fourier transform infrared spectrum?
    • Khurana, R., and Fink, A. L. (2000) Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophys. J. 78, 994-1000.
    • (2000) Biophys. J. , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 33
    • 0023118252 scopus 로고
    • Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer's disease
    • Selkoe, D. J., Bell, D. S., Podlisny, M. B., Price, D. L., and Cork, L. C. (1987) Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer's disease. Science 235, 873-877.
    • (1987) Science , vol.235 , pp. 873-877
    • Selkoe, D.J.1    Bell, D.S.2    Podlisny, M.B.3    Price, D.L.4    Cork, L.C.5
  • 35
    • 80052962449 scopus 로고    scopus 로고
    • Behavioural and cellular effects of exogenous amyloid-β peptides in rodents
    • Chambon, C., Wegener, N., Gravius, A., and Danysz, W. (2011) Behavioural and cellular effects of exogenous amyloid-β peptides in rodents. Behav. Brain Res. 225, 623-641.
    • (2011) Behav. Brain Res. , vol.225 , pp. 623-641
    • Chambon, C.1    Wegener, N.2    Gravius, A.3    Danysz, W.4
  • 36
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • Nanga, R. P., Brender, J. R., Xu, J., Hartman, K., Subramanian, V., and Ramamoorthy, A. (2009) Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J. Am. Chem. Soc. 131, 8252-8261.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8252-8261
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Hartman, K.4    Subramanian, V.5    Ramamoorthy, A.6
  • 37
    • 84858632761 scopus 로고    scopus 로고
    • Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
    • Brender, J. R., Salamekh, S., and Ramamoorthy, A. (2012) Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective. Acc. Chem. Res. 45, 454-462.
    • (2012) Acc. Chem. Res. , vol.45 , pp. 454-462
    • Brender, J.R.1    Salamekh, S.2    Ramamoorthy, A.3
  • 38
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13
    • Williamson, M. P., Suzuki, Y., Bourne, N. T., and Asakura, T. (2006) Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13. Biochem. J. 397, 483-490.
    • (2006) Biochem. J. , vol.397 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 39
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • Coles, M., Bicknell, W., Watson, A. A., Fairlie, D. P., and Craik, D. J. (1998) Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry 37, 11064-11077.
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 40
    • 0033555275 scopus 로고    scopus 로고
    • Solution structure of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer' s disease
    • Shao, H., Jao, S.-C., Ma, K., and Zagorski, M. G. (1999) Solution structure of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer' s disease. J. Mol. Biol. 285, 755-773.
    • (1999) J. Mol. Biol. , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.-C.2    Ma, K.3    Zagorski, M.G.4
  • 41
    • 34547920308 scopus 로고    scopus 로고
    • Positioning of the Alzheimer Aβ (1-40) peptide in SDS micelles using NMR and paramagnetic probes
    • Jarvet, J., Danielsson, J., Damberg, P., Oleszczuk, M., and Graslund, A. (2007) Positioning of the Alzheimer Aβ (1-40) peptide in SDS micelles using NMR and paramagnetic probes. J. Biomol. NMR 39, 63-72.
    • (2007) J. Biomol. NMR , vol.39 , pp. 63-72
    • Jarvet, J.1    Danielsson, J.2    Damberg, P.3    Oleszczuk, M.4    Graslund, A.5
  • 42
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • Utsumi, M., Yamaguchi, Y., Sasakawa, H., Yamamoto, N., Yanagisawa, K., and Kato, K. (2008) Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters. Glycoconjugate J. 26, 999-1006.
    • (2008) Glycoconjugate J. , vol.26 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 43
    • 34547118151 scopus 로고    scopus 로고
    • Formation of amyloids by Aβ-(1-42) on NGF-differentiated PC12 cells: Roles of gangliosides and cholesterol
    • Wakabayashi, M., and Matsuzaki, K. (2007) Formation of amyloids by Aβ-(1-42) on NGF-differentiated PC12 cells: Roles of gangliosides and cholesterol. J. Mol. Biol. 371, 924-933.
    • (2007) J. Mol. Biol. , vol.371 , pp. 924-933
    • Wakabayashi, M.1    Matsuzaki, K.2
  • 44
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a β-pleated sheet conformation
    • Klunk, W. E., Pettegrew, J. W., and Abraham, D. J. (1989) Quantitative evaluation of Congo red binding to amyloid-like proteins with a β-pleated sheet conformation. J. Histochem. Cytochem. 37, 1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 45
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • Biancalana, M., and Koide, S. (2010) Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim. Biophys. Acta 1804, 1405-1412.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 46
    • 84860390157 scopus 로고    scopus 로고
    • In vivo and in vitro analyses of toxic mutants of HET-s: FTIR antiparallel signature correlates with amyloid toxicity
    • Berthelot, K., Ta, H. P., Géan, J., Lecomte, S., and Cullin, C. (2011) In vivo and in vitro analyses of toxic mutants of HET-s: FTIR antiparallel signature correlates with amyloid toxicity. J. Mol. Biol. 412, 137-152.
    • (2011) J. Mol. Biol. , vol.412 , pp. 137-152
    • Berthelot, K.1    Ta, H.P.2    Géan, J.3    Lecomte, S.4    Cullin, C.5
  • 47
  • 48
    • 0035105932 scopus 로고    scopus 로고
    • Say NO to Alzheimer's disease: The putative links between nitric oxide and dementia of the Alzheimer's type
    • Law, A., Gauthier, S., and Quirion, R. (2001) Say NO to Alzheimer's disease: The putative links between nitric oxide and dementia of the Alzheimer's type. Brain Res. Rev. 35, 73-96.
    • (2001) Brain Res. Rev. , vol.35 , pp. 73-96
    • Law, A.1    Gauthier, S.2    Quirion, R.3
  • 49
    • 0029935694 scopus 로고    scopus 로고
    • Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes in mice
    • Igbavboa, U., Avdulov, N. A., Schroeder, F., and Wood, W. G. (1996) Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes in mice. J. Neurochem. 66, 1717-1725.
    • (1996) J. Neurochem. , vol.66 , pp. 1717-1725
    • Igbavboa, U.1    Avdulov, N.A.2    Schroeder, F.3    Wood, W.G.4
  • 50
    • 0037171006 scopus 로고    scopus 로고
    • Cholesterol is increased in the exofacial leaflet of synaptic plasma membranes of human apolipoprotein E4 knock-in mice
    • Hayashi, H., Igbavboa, U., Hamanaka, H., Kobayashi, M., Fujita, S. C., Wood, W. G., and Yanagisawa, K. (2002) Cholesterol is increased in the exofacial leaflet of synaptic plasma membranes of human apolipoprotein E4 knock-in mice. NeuroReport 13, 383-386.
    • (2002) NeuroReport , vol.13 , pp. 383-386
    • Hayashi, H.1    Igbavboa, U.2    Hamanaka, H.3    Kobayashi, M.4    Fujita, S.C.5    Wood, W.G.6    Yanagisawa, K.7
  • 51
    • 55749095544 scopus 로고    scopus 로고
    • Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid β-protein fibrillogenesis
    • Yamamoto, N., Matsubara, T., Sato, T., and Yanagisawa, K. (2008) Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid β-protein fibrillogenesis. Biochim. Biophys. Acta 1778, 2717-2726.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2717-2726
    • Yamamoto, N.1    Matsubara, T.2    Sato, T.3    Yanagisawa, K.4
  • 52
    • 0025002019 scopus 로고
    • Alzheimer patients and Down patients: Abnormal presynaptic terminals are related to cerebral preamyloid deposits
    • Bugiani, O., Giaccone, G., Verga, L., Pollo, B., Ghetti, B., Frangione, B., and Tagliavini, F. (1990) Alzheimer patients and Down patients: Abnormal presynaptic terminals are related to cerebral preamyloid deposits. Neurosci. Lett. 119, 56-59.
    • (1990) Neurosci. Lett. , vol.119 , pp. 56-59
    • Bugiani, O.1    Giaccone, G.2    Verga, L.3    Pollo, B.4    Ghetti, B.5    Frangione, B.6    Tagliavini, F.7
  • 53
    • 0026042933 scopus 로고
    • Deposition of β/A4 protein along neuronal plasma membranes in diffuse senile plaques
    • Probst, A., Langui, D., Ipsen, S., Robakis, N., and Ulrich, J. (1991) Deposition of β/A4 protein along neuronal plasma membranes in diffuse senile plaques. Acta Neuropathol. 83, 21-29.
    • (1991) Acta Neuropathol. , vol.83 , pp. 21-29
    • Probst, A.1    Langui, D.2    Ipsen, S.3    Robakis, N.4    Ulrich, J.5
  • 55
    • 33750328015 scopus 로고    scopus 로고
    • Further evidence of local ganglioside-dependent amyloid β-protein assembly in brain
    • Yamamoto, N., Van Nostrand, W. E., and Yanagisawa, K. (2006) Further evidence of local ganglioside-dependent amyloid β-protein assembly in brain. NeuroReport 17, 1735-1737.
    • (2006) NeuroReport , vol.17 , pp. 1735-1737
    • Yamamoto, N.1    Van Nostrand, W.E.2    Yanagisawa, K.3
  • 57
    • 25144505865 scopus 로고    scopus 로고
    • Suppression of Aβ deposition in brain by peripheral administration of Fab fragments of anti-seed antibody
    • Yamamoto, N., Yokoseki, T., Shibata, M., Yamaguchi, H., and Yanagisawa, K. (2005) Suppression of Aβ deposition in brain by peripheral administration of Fab fragments of anti-seed antibody. Biochem. Biophys. Res. Commun. 335, 45-47.
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 45-47
    • Yamamoto, N.1    Yokoseki, T.2    Shibata, M.3    Yamaguchi, H.4    Yanagisawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.