메뉴 건너뛰기




Volumn 287, Issue 46, 2012, Pages 38992-39000

A novel inhibitor of amyloid β (Aβ) peptide aggregation: From high throughput screening to efficacy in an animal model of Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; GLYCOPROTEINS; NEURODEGENERATIVE DISEASES; OLIGOMERS; PEPTIDES; TOXICITY;

EID: 84869016210     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.348037     Document Type: Article
Times cited : (92)

References (38)
  • 1
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • Alexandrescu, A. (2005) Amyloid accomplices and enforcers. Protein Sci. 14, 1-12
    • (2005) Protein Sci. , vol.14 , pp. 1-12
    • Alexandrescu, A.1
  • 2
    • 0034961205 scopus 로고    scopus 로고
    • The amyloid-β peptide and its role in Alzheimer's disease
    • DOI 10.1002/psc.324
    • Clippingdale, A. B., Wade, J. D., and Barrow, C. J. (2001) The amyloid β peptide and its role in Alzheimer disease. J. Pept. Sci. 7, 227-249 (Pubitemid 32586583)
    • (2001) Journal of Peptide Science , vol.7 , Issue.5 , pp. 227-249
    • Clippingdale, A.B.1    Wade, J.D.2    Barrow, C.J.3
  • 3
    • 0036403702 scopus 로고    scopus 로고
    • Deciphering the genetic basis of Alzheimer's disease
    • DOI 10.1146/annurev.genom.3.022502.103022
    • Selkoe, D. J., and Podlisny, M. B. (2002) Deciphering the genetic basis of Alzheimer disease. Annu. Rev. Genomics Hum. Genet. 3, 67-99 (Pubitemid 35217431)
    • (2002) Annual Review of Genomics and Human Genetics , vol.3 , pp. 67-99
    • Selkoe, D.J.1    Podlisny, M.B.2
  • 4
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
    • DOI 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe, D. J, and Schenk, D. (2003) Alzheimer disease: molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. 43, 545-584 (Pubitemid 37372653)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 5
    • 0026597063 scopus 로고
    • Alzheimer disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (1992) Alzheimer disease: the amyloid cascade hypothesis. Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 6
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer disease: Genes, proteins, and therapy
    • Selkoe, D. (2001) Alzheimer disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.1
  • 7
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer disease: Strategies for disease modification
    • Citron, M. (2010) Alzheimer disease: strategies for disease modification. Nat. Rev. Drug Discov. 9, 387-398
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 387-398
    • Citron, M.1
  • 8
    • 2942561028 scopus 로고    scopus 로고
    • The importance of neuritic plaques and tangles to the development and evolution of AD
    • Tiraboschi, P., Hansen, L. A., Thal, L. J., Corey-Bloom, J. (2004) The importance of neuritic plaques and tangles to the development and evolution of AD. Neurology 62, 1984-1989 (Pubitemid 38738208)
    • (2004) Neurology , vol.62 , Issue.11 , pp. 1984-1989
    • Tiraboschi, P.1    Hansen, L.A.2    Thal, L.J.3    Corey-Bloom, J.4
  • 10
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the etiology of Alzheimer disease
    • Hardy, J., and Allsop, D. (1991) Amyloid deposition as the central event in the etiology of Alzheimer disease. Trends Pharmacol. Sci. 12, 383-388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 11
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J., and Selkoe, D. (2002) The amyloid hypothesis of Alzheimer disease: progress and problems on the road to therapeutics. Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 12
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007) Aβ oligomers - a decade of discovery. J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 13
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • Walsh, D. M., and Selkoe, D. J. (2004) Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11, 213-228 (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 14
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C. (2008) Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283, 29639-29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.1
  • 15
    • 67650690570 scopus 로고    scopus 로고
    • Protective effects of Ginkgo biloba extract (EGb761) and its constituents quercetin and ginkgolide B against β-amyloid peptide-induced toxicity in SH-SY5Y cells
    • Shi, C., Zhao, L., Zhu, B., Li, Q., Yew, D. T., Yao, Z., and Xu, J. (2009) Protective effects of Ginkgo biloba extract (EGb761) and its constituents quercetin and ginkgolide B against β-amyloid peptide-induced toxicity in SH-SY5Y cells. Chem. Biol. Interact. 181, 115-123
    • (2009) Chem. Biol. Interact. , vol.181 , pp. 115-123
    • Shi, C.1    Zhao, L.2    Zhu, B.3    Li, Q.4    Yew, D.T.5    Yao, Z.6    Xu, J.7
  • 16
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 17
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 18
    • 33750449952 scopus 로고    scopus 로고
    • A high throughput screen for compounds that inhibit aggregation of the Alzheimer peptide
    • Kim, W., Kim, Y., Min, J., Kim, D. J., Chang, Y. T., and Hecht, M. H. (2006) A high throughput screen for compounds that inhibit aggregation of the Alzheimer peptide. ACS Chem. Biol. 1, 461-469
    • (2006) ACS Chem. Biol. , vol.1 , pp. 461-469
    • Kim, W.1    Kim, Y.2    Min, J.3    Kim, D.J.4    Chang, Y.T.5    Hecht, M.H.6
  • 19
    • 0033015460 scopus 로고    scopus 로고
    • Rapid protein-folding assay using green fluorescent protein
    • DOI 10.1038/10904
    • Waldo, G. S., Standish, B. M., Berendzen, J., and Terwilliger, T. C. (1999) Rapid protein-folding assay using green fluorescent protein. Nat. Biotechnol. 17, 691-695 (Pubitemid 29316148)
    • (1999) Nature Biotechnology , vol.17 , Issue.7 , pp. 691-695
    • Waldo, G.S.1    Standish, B.M.2    Berendzen, J.3    Terwilliger, T.C.4
  • 21
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., 3rd (1993) Thioflavin T interaction with synthetic Alzheimer disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 22
    • 33745272215 scopus 로고    scopus 로고
    • Physiochemical characterization of the Alzheimer disease-related peptides Aβ1-42Arctic and A β1-42wt
    • Johansson, A. S., Berglind-Dehlin, F., Karlsson, G., Edwards, K., Gellerfors, P., and Lannfelt, L. (2006) Physiochemical characterization of the Alzheimer disease-related peptides Aβ1-42Arctic and A β1-42wt. FEBS J. 273, 2618-2630
    • (2006) FEBS J. , vol.273 , pp. 2618-2630
    • Johansson, A.S.1    Berglind-Dehlin, F.2    Karlsson, G.3    Edwards, K.4    Gellerfors, P.5    Lannfelt, L.6
  • 23
    • 33947719234 scopus 로고    scopus 로고
    • Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway
    • DOI 10.1110/ps.062514807
    • Lee, S., Fernandez, E. J., and Good, T. A. (2007) Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway. Protein Sci. 16, 723-732 (Pubitemid 46507001)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 723-732
    • Lee, S.1    Fernandez, E.J.2    Good, T.A.3
  • 27
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 28
    • 33747823312 scopus 로고    scopus 로고
    • Ginkgo biloba and donepezil: A comparison in the treatment of Alzheimer's dementia in a randomized placebo-controlled double-blind study
    • DOI 10.1111/j.1468-1331.2006.01409.x
    • Mazza, M., Capuano, A., Bria, P., and Mazza, S. (2006) Ginkgo biloba and donepezil: a comparison in the treatment of Alzheimer dementia in a randomized placebo-controlled double-blind study. Eur. J. Neurol. 13, 981-985 (Pubitemid 44284905)
    • (2006) European Journal of Neurology , vol.13 , Issue.9 , pp. 981-985
    • Mazza, M.1    Capuano, A.2    Bria, P.3    Mazza, S.4
  • 29
    • 0035910374 scopus 로고    scopus 로고
    • The Ginkgo biloba extract EGb 761 rescues the PC12 neuronal cells from β-amyloid-induced cell death by inhibiting the formation of β-amyloid-derived diffusible neurotoxic ligands
    • DOI 10.1016/S0006-8993(00)03131-0, PII S0006899300031310
    • Yao, Z., Drieu, K., and Papadopoulos, V. (2001) The Ginkgo biloba extract EGb761 rescues the PC12 neuronal cells from β-amyloid-induced cell death by inhibiting the formation of β-amyloid-derived diffusible neurotoxic ligands. Brain Res. 889, 181-190 (Pubitemid 32146280)
    • (2001) Brain Research , vol.889 , Issue.1-2 , pp. 181-190
    • Yao, Z.-X.1    Drieu, K.2    Papadopoulos, V.3
  • 31
    • 70349385343 scopus 로고    scopus 로고
    • Protective effect of a tri-azine- derivative (AA3E2) on β-amyloid-induced damages in SK-N-MC cells
    • Yazdanparast, R., and Shaykhalishahi, H. (2009) Protective effect of a tri-azine- derivative (AA3E2) on β-amyloid-induced damages in SK-N-MC cells. Toxicol. in Vitro 23, 1277-1283
    • (2009) Toxicol. in Vitro , vol.23 , pp. 1277-1283
    • Yazdanparast, R.1    Shaykhalishahi, H.2
  • 32
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • DOI 10.1016/j.neuroscience.2004.12.025
    • Crowther, D. C., Kinghorn, K. J., Miranda, E., Page, R., Curry, J. A., Duthie, F. A., Gubb, D. C., and Lomas, D. A. (2005) Intraneuronal Aβ, nonamyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer disease. Neuroscience 132, 123-135 (Pubitemid 40380720)
    • (2005) Neuroscience , vol.132 , Issue.1 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3    Page, R.4    Curry, J.A.5    Duthie, F.A.I.6    Gubb, D.C.7    Lomas, D.A.8
  • 33
    • 79955749505 scopus 로고    scopus 로고
    • Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery
    • Pandey, U. B., and Nichols, C. D. (2011) Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery. Pharmacol. Rev. 63, 411-436
    • (2011) Pharmacol. Rev. , vol.63 , pp. 411-436
    • Pandey, U.B.1    Nichols, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.