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Volumn 251, Issue 1, 1998, Pages 65-68

The inhibitory effect of laminin 1 and synthetic peptides deduced from the sequence in the laminin α1 chain on Aβ40 fibril formation in vitro

Author keywords

Alzheimer's disease; Amyloid protein; Electron microscopy; Laminin; Synthetic peptides; Thioflavine T fluorescence

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; LAMININ; SYNTHETIC PEPTIDE; THIOFLAVINE;

EID: 0032541019     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(98)00499-6     Document Type: Article
Times cited : (13)

References (19)
  • 1
    • 0029661902 scopus 로고    scopus 로고
    • α-1-Antichymotrypsin interaction with Aβ(1-40) inhibits fibril formation but does not affect the peptide toxicity
    • Aksenova M.V., Aksenov M.Y., Butterfield D.A., Carney J.M. α-1-Antichymotrypsin interaction with Aβ(1-40) inhibits fibril formation but does not affect the peptide toxicity. Neurosci. Lett. 211:1996;45-48.
    • (1996) Neurosci. Lett. , vol.211 , pp. 45-48
    • Aksenova, M.V.1    Aksenov, M.Y.2    Butterfield, D.A.3    Carney, J.M.4
  • 2
    • 0029969354 scopus 로고    scopus 로고
    • Glutamate synthetase-induced enhancement of β-amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation
    • Aksenov M.Y., Aksenova M.Y., Butterfield D.A., Hensley K., Vigo-Pelfrey C., Carney J.M. Glutamate synthetase-induced enhancement of β-amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation. J. Neurochem. 66:1996;2050-2056.
    • (1996) J. Neurochem. , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.Y.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 4
    • 0030061861 scopus 로고    scopus 로고
    • Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments
    • Bronfman F.C., Soto C., Tapia L., Tapia V., Inestrosa N.C. Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments. J. Cell. Physiol. 166:1996;360-369.
    • (1996) J. Cell. Physiol. , vol.166 , pp. 360-369
    • Bronfman, F.C.1    Soto, C.2    Tapia, L.3    Tapia, V.4    Inestrosa, N.C.5
  • 5
    • 0029910347 scopus 로고    scopus 로고
    • A strategy for designing inhibitors of β-amyloid toxicity
    • Ghanta J., Shen C.-L., Kiessling L.L., Murphy R.M. A strategy for designing inhibitors of β-amyloid toxicity. J. Biol. Chem. 271:1996;29525-29528.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29525-29528
    • Ghanta, J.1    Shen, C.-L.2    Kiessling, L.L.3    Murphy, R.M.4
  • 6
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;76-83.
    • (1993) Protein Sci. , vol.2 , pp. 76-83
    • Levine, H.1
  • 7
    • 0031053932 scopus 로고    scopus 로고
    • Laminin and the mechanism of neuronal outgrowth
    • Luckenbill-Edds L. Laminin and the mechanism of neuronal outgrowth. Brain Res. Rev. 23:1997;1-27.
    • (1997) Brain Res. Rev. , vol.23 , pp. 1-27
    • Luckenbill-Edds, L.1
  • 8
    • 0026716274 scopus 로고
    • Laminin and its neurite outgrowth-promoting domain in the brain of Alzheimer's disease and Down's syndrome patients
    • Murtomaki S., Risteri J., Risteri L., Koivisto U.M., Johansson S., Liesi P. Laminin and its neurite outgrowth-promoting domain in the brain of Alzheimer's disease and Down's syndrome patients. J. Neurosci. Res. 32:1992;261-273.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 261-273
    • Murtomaki, S.1    Risteri, J.2    Risteri, L.3    Koivisto, U.M.4    Johansson, S.5    Liesi, P.6
  • 9
    • 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. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13:1993;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
  • 11
    • 0029916711 scopus 로고    scopus 로고
    • The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis
    • Soto C., Castano E.M. The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis. Biochem. J. 314:1996;701-707.
    • (1996) Biochem. J. , vol.314 , pp. 701-707
    • Soto, C.1    Castano, E.M.2
  • 12
    • 0029865644 scopus 로고    scopus 로고
    • Alzheimer's β-amyloid peptide is conformationally modified by apolipoprotein E in vitro
    • Soto C., Golabek A., Wisniewski T., Castano E.M. Alzheimer's β-amyloid peptide is conformationally modified by apolipoprotein E in vitro. NeuroReport. 7:1996;721-725.
    • (1996) NeuroReport , vol.7 , pp. 721-725
    • Soto, C.1    Golabek, A.2    Wisniewski, T.3    Castano, E.M.4
  • 13
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • Soto C., Kindy M.S., Baumann M., Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Commun. 226:1996;672-680.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 14
    • 0024443667 scopus 로고
    • A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth
    • Tashiro K., Sephel G.C., Weeks B., Sasaki M., Martin G.R., Kleinman H.K., Yamada Y. A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth. J. Biol. Chem. 264:1989;16174-16182.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16174-16182
    • Tashiro, K.1    Sephel, G.C.2    Weeks, B.3    Sasaki, M.4    Martin, G.R.5    Kleinman, H.K.6    Yamada, Y.7
  • 15
    • 0028086515 scopus 로고
    • A synthetic peptide deduced from the sequence in the cross-region of laminin A chain mediates neurite outgrowth, cell attachment and heparin binding
    • Tashiro K., Nagata I., Yamashita N., Okazaki K., Ogomori K., Tashiro N., Anai M. A synthetic peptide deduced from the sequence in the cross-region of laminin A chain mediates neurite outgrowth, cell attachment and heparin binding. Biochem. J. 302:1994;73-79.
    • (1994) Biochem. J. , vol.302 , pp. 73-79
    • Tashiro, K.1    Nagata, I.2    Yamashita, N.3    Okazaki, K.4    Ogomori, K.5    Tashiro, N.6    Anai, M.7
  • 18
    • 0030918418 scopus 로고    scopus 로고
    • Aggregation-state dependent activation of the classical complement pathway by the amyloid β peptide
    • Webster S., Bradt B., Rogers J., Cooper N. Aggregation-state dependent activation of the classical complement pathway by the amyloid β peptide. J. Neurochem. 69:1997;388-398.
    • (1997) J. Neurochem. , vol.69 , pp. 388-398
    • Webster, S.1    Bradt, B.2    Rogers, J.3    Cooper, N.4
  • 19
    • 0029896354 scopus 로고    scopus 로고
    • Mechanism of neuronal degeneration in Alzheimer's disease
    • Yanker B.A. Mechanism of neuronal degeneration in Alzheimer's disease. Neuron. 16:1996;921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yanker, B.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.