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Volumn 328, Issue 4, 2005, Pages 816-823

A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by β-amyloid (1-42)

Author keywords

Inhibitor for toxic amyloid peptide; Synthesis of styryl benzene ferulic acid hybrid molecules

Indexed keywords

1,3 BIS(2',4' DIMETHOXYSTYRYL)BENZENE; 1,3 BIS(3' METHOXY 4' HYDROXYSTYRYL)BENZENE; 1,3 BIS(3',4' DIMETHOXYSTYRYL)BENZENE; AMYLOID BETA PROTEIN[1-42]; BENZENE DERIVATIVE; FERULIC ACID; NOOTROPIC AGENT; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 13744252140     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.01.030     Document Type: Article
Times cited : (36)

References (26)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe 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
  • 2
    • 0036639707 scopus 로고    scopus 로고
    • Novel therapeutic strategies provide the real test for the amyloid hypothesis of Alzheimer's disease
    • D.I. Domingues, and B.D. Stooper Novel therapeutic strategies provide the real test for the amyloid hypothesis of Alzheimer's disease Trends Pharmacol. Sci. 23 2002 324 330
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 324-330
    • Domingues, D.I.1    Stooper, B.D.2
  • 3
    • 0036242449 scopus 로고    scopus 로고
    • Advances in the development of Abeta-related therapeutic strategies for Alzheimer's disease
    • C.J. Barrow Advances in the development of Abeta-related therapeutic strategies for Alzheimer's disease Drug News Perspect. 15 2002 102 109
    • (2002) Drug News Perspect. , vol.15 , pp. 102-109
    • Barrow, C.J.1
  • 4
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, M.S. Wolfe, M.J. Rowan, and D.J. Selkoe Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, 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
  • 5
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric a beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Y. Gong, L. Chang, K.L. Viola, P.L. Lacor, M.P. Lambert, C.E. Finch, G.A. Krafft, and W.L. Klein Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc. Natl. Acad. Sci. USA 100 2003 10417 10422
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.L.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 6
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • M.D. Kirkitadze, G. Bitan, and D.B. Teplow Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies J. Neurosci. Res. 69 2002 567 577
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 7
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • I. Sanchez, C. Mahlke, and J. Yuan Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders Nature 421 2003 373 379
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 8
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • P. Hammarstrom, R.L. Wiseman, E.T. Powers, and J.W. Kelly Prevention of transthyretin amyloid disease by changing protein misfolding energetics Science 299 2003 713 716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 9
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • G. Bitan, A. Lomakin, and D.B. Teplow Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins J. Biol. Chem. 276 2001 35176 35184
    • (2001) J. Biol. Chem. , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 12
    • 0036860355 scopus 로고    scopus 로고
    • Amyloid binding ligands as Alzheimer's disease therapies
    • V.M. Lee Amyloid binding ligands as Alzheimer's disease therapies Neurobiol. Aging 23 2002 1039 1042
    • (2002) Neurobiol. Aging , vol.23 , pp. 1039-1042
    • Lee, V.M.1
  • 14
    • 0034839145 scopus 로고    scopus 로고
    • Effect of the Alzheimer amyloid fragment Abeta(25-35) on Akt/PKB kinase and survival of PC12 cells
    • D. Martin, M. Salinas, R. Lopez-Valdaliso, E. Serrano, M. Recuero, and A. Cuadrado Effect of the Alzheimer amyloid fragment Abeta(25-35) on Akt/PKB kinase and survival of PC12 cells J. Neurochem. 78 2001 1000 1008
    • (2001) J. Neurochem. , vol.78 , pp. 1000-1008
    • Martin, D.1    Salinas, M.2    Lopez-Valdaliso, R.3    Serrano, E.4    Recuero, M.5    Cuadrado, A.6
  • 15
    • 0346492847 scopus 로고    scopus 로고
    • Method for measuring neurotoxicity of aggregating polypeptides with the MTT assay on differentiated neuroblastoma cells
    • Z. Datki, A. Juhasz, M. Galfi, K. Soos, R. Papp, D. Zadori, and B. Penke Method for measuring neurotoxicity of aggregating polypeptides with the MTT assay on differentiated neuroblastoma cells Brain Res. Bull. 62 2003 223 229
    • (2003) Brain Res. Bull. , vol.62 , pp. 223-229
    • Datki, Z.1    Juhasz, A.2    Galfi, M.3    Soos, K.4    Papp, R.5    Zadori, D.6    Penke, B.7
  • 16
    • 0036667331 scopus 로고    scopus 로고
    • 4,4(′)-Dianilino-1,1(′)-binaphthyl-5,5(′)-disulfonate: Report on non-beta-sheet conformers of Alzheimer's peptide beta (1-40)
    • H. LeVine III 4,4(′)-Dianilino-1,1(′)-binaphthyl-5,5(′) -disulfonate: report on non-beta-sheet conformers of Alzheimer's peptide beta (1-40) Arch. Biochem. Biophys. 404 2002 106 115
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 106-115
    • LeVine III, H.1
  • 17
    • 0036444474 scopus 로고    scopus 로고
    • In vitro fibrillogenesis of the amyloid beta 1-42 peptide: Cholesterol potentiation and aspirin inhibition
    • J.R. Harris In vitro fibrillogenesis of the amyloid beta 1-42 peptide: cholesterol potentiation and aspirin inhibition Micron 33 2002 609 626
    • (2002) Micron , vol.33 , pp. 609-626
    • Harris, J.R.1
  • 19
    • 0038017237 scopus 로고    scopus 로고
    • Study on the optical properties of 4,4′-bis-(2-(substituted-styryl) )biphenyl and 1,4-bis-(2-(substituted-styryl))benzene
    • H.C. Song, W.M. Li, G.R. Liu, and Z.L. Xu Study on the optical properties of 4,4′-bis-(2-(substituted-styryl))biphenyl and 1,4-bis-(2-(substituted- styryl))benzene Spectrochim. Acta A Mol. Biomol. Spectrosc. 59 2003 2041 2048
    • (2003) Spectrochim. Acta a Mol. Biomol. Spectrosc. , vol.59 , pp. 2041-2048
    • Song, H.C.1    Li, W.M.2    Liu, G.R.3    Xu, Z.L.4
  • 21
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • S.L. McGovern, E. Caselli, N. Grigorieff, and B.K. Shoichet A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening J. Med. Chem. 45 2002 1712 1722
    • (2002) J. Med. Chem. , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 22
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) for of Aβ40 in vitro accumulate protofibrils, including amyloid pores
    • H.A. Lashuel, D.M. Hartley, B.M. Petre, J.S. Wall, M.N. Simon, T. Walz, and P.T. Lansbury Jr. Mixtures of wild-type and a pathogenic (E22G) for of Aβ40 in vitro accumulate protofibrils, including amyloid pores J. Mol. Biol. 332 2003 795 808
    • (2003) J. Mol. Biol. , vol.332 , pp. 795-808
    • Lashuel, H.A.1    Hartley, D.M.2    Petre, B.M.3    Wall, J.S.4    Simon, M.N.5    Walz, T.6    Lansbury Jr., P.T.7
  • 23
    • 0037319127 scopus 로고    scopus 로고
    • Secondary conformations and temperature effect on structural transformation of amyloid beta (1-28), (1-40) and (1-42) peptides
    • S.Y. Lin, H.L. Chu, and Y.S. Wei Secondary conformations and temperature effect on structural transformation of amyloid beta (1-28), (1-40) and (1-42) peptides J. Biomol. Struct. Dyn. 20 2003 595 601
    • (2003) J. Biomol. Struct. Dyn. , vol.20 , pp. 595-601
    • Lin, S.Y.1    Chu, H.L.2    Wei, Y.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.