메뉴 건너뛰기




Volumn 287, Issue 24, 2012, Pages 20748-20754

Expression in Drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; GLYCOPROTEINS; OLIGOMERS; TOXICITY;

EID: 84862003761     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.350124     Document Type: Article
Times cited : (39)

References (29)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution, and disease
    • Dobson, C. M. (1999) Protein misfolding, evolution, and disease. Trends Biochem. Sci. 24, 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 5
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • DOI 10.1016/j.abb.2007.05.015, PII S0003986107002731, Highlight Issue: Protein Folding
    • Jahn, T. R., and Radford, S. E. (2008) Folding versus aggregation: polypeptide conformations on competing pathways. Arch. Biochem. Biophys. 469, 100-117 (Pubitemid 350214559)
    • (2008) Archives of Biochemistry and Biophysics , vol.469 , Issue.1 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 6
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G., and Wong, C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890 (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 7
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1021/bi00069a001
    • Jarrett, J. T., Berger, E. P., and Lansbury, P. T., Jr. (1993) The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 13
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    • DOI 10.1016/j.jmb.2005.11.034, PII S0022283605014221
    • Bader, R., Bamford, R., Zurdo, J., Luisi, B. F., and Dobson, C. M. (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. J. Mol. Biol. 356, 189-208 (Pubitemid 43069737)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.1 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 14
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • DOI 10.1038/nature04195
    • Wright, C. F., Teichmann, S. A., Clarke, J., and Dobson, C. M. (2005) The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438, 878-881 (Pubitemid 41753072)
    • (2005) Nature , vol.438 , Issue.7069 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 20
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid β protein oligomers
    • Ono, K., Condron, M. M., and Teplow, D. B. (2009) Structure-neurotoxicity relationships of amyloid β protein oligomers. Proc. Natl. Acad. Sci. U.S.A. 106, 14745-14750
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 22
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic, J. L., Pensalfini, A., Head, E., and Glabe, C. G. (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol. Dis. 35, 352-358
    • (2009) Neurobiol. Dis. , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 25
    • 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
  • 26
    • 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. J. (2002) The amyloid hypothesis of Alzheimer's 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
  • 28
    • 0033762437 scopus 로고    scopus 로고
    • The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2
    • Green, C., Levashina, E., McKimmie, C., Dafforn, T., Reichhart, J. M., and Gubb, D. (2000) The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2. Genetics 156, 1117-1127
    • (2000) Genetics , vol.156 , pp. 1117-1127
    • Green, C.1    Levashina, E.2    McKimmie, C.3    Dafforn, T.4    Reichhart, J.M.5    Gubb, D.6
  • 29
    • 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, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.