메뉴 건너뛰기




Volumn 18, Issue 12, 2004, Pages 1366-1372

Targeting the neurotoxic species in Alzheimer's disease: Inhibitors of Aβ oligomerization

Author keywords

Amyloid; Neuroprotection; Oligomers; Small molecule inhibitors

Indexed keywords

2 AMINO 4 CHLOROPHENOL; 2 HYDROXY 3 ETHOXYBENZALDEHYDE; 4 AMINOPHENOL; AMYLOID; AMYLOID BETA PROTEIN; AROMATIC COMPOUND; NEUROPROTECTIVE AGENT; NEUROTOXIN; OLIGOMER; PARA ANISIDINE; PROTOCATECHUIC ACID; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 4344688011     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.04-1764com     Document Type: Article
Times cited : (179)

References (44)
  • 1
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer's disease - Proteolysis holds the key
    • Haass, C., and De Strooper, B. (1999) The presenilins in Alzheimer's disease - proteolysis holds the key. Science 286, 916-919
    • (1999) Science , vol.286 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 2
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D. J. (2002) Alzheimer's disease is a synaptic failure. Science 298, 789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 3
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yankner, B. A. (2000) Apoptosis in the nervous system. Nature (London) 407, 802-809
    • (2000) Nature (London) , vol.407 , pp. 802-809
    • Yankner, B.A.1
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B., and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 5
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G., and Cotman, C. W. (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 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
  • 6
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo, A., and Yankner, B. A. (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. USA 91, 12243-12247
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 7
    • 0037130570 scopus 로고    scopus 로고
    • Characterization of neuronal dystrophy induced by fibrillar amyloid beta: Implications for Alzheimer's disease
    • Grace, E. A., Rabiner, C. A., and Busciglio, J. (2002) Characterization of neuronal dystrophy induced by fibrillar amyloid beta: implications for Alzheimer's disease. Neuroscience 114, 265-273
    • (2002) Neuroscience , vol.114 , pp. 265-273
    • Grace, E.A.1    Rabiner, C.A.2    Busciglio, J.3
  • 10
    • 0036669881 scopus 로고    scopus 로고
    • Amyloid-beta oligomers: Their production, toxicity and therapeutic inhibition
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Rowan, M. J., and Selkoe, D. J. (2002) Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition. Biochem. Soc. Trans. 30, 552-557
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 552-557
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Rowan, M.J.4    Selkoe, D.J.5
  • 12
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 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
    • (2003) Science , vol.300 , 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    Glabe, C.G.7
  • 13
    • 0036975682 scopus 로고    scopus 로고
    • Beta-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease
    • De Felice, F. G., and Ferreira, S. T. (2002) Beta-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease. Cell. Mol. Neurobiol. 22, 545-563
    • (2002) Cell. Mol. Neurobiol. , vol.22 , pp. 545-563
    • De Felice, F.G.1    Ferreira, S.T.2
  • 14
    • 0037044835 scopus 로고    scopus 로고
    • New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease
    • Lashuel, H. A., Hartley, D. M., Balakhaneh, D., Aggarwal, A., Teichberg, S., and Callaway, D. J. (2002) New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. J. Biol. Chem. 277, 42881-42890
    • (2002) J. Biol. Chem. , vol.277 , pp. 42881-42890
    • Lashuel, H.A.1    Hartley, D.M.2    Balakhaneh, D.3    Aggarwal, A.4    Teichberg, S.5    Callaway, D.J.6
  • 15
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • Li, J., Zhu, M., Manning-Bog, A. B., Di Monte, D. A., and Fink, A. L. (2004) Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J. 18, 962-964
    • (2004) FASEB J. , vol.18 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 16
    • 1242316922 scopus 로고    scopus 로고
    • Abeta aggregation inhibitors. Synthesis and biological activity of phenylazo benzenesulfonamides
    • Lin, S. J., Shiao, Y. J., Chi, C. W., and Yang, L. M. (2004) Abeta aggregation inhibitors. Synthesis and biological activity of phenylazo benzenesulfonamides. Bioorg. Med. Chem. Lett. 14, 1173-1176
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 1173-1176
    • Lin, S.J.1    Shiao, Y.J.2    Chi, C.W.3    Yang, L.M.4
  • 17
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro
    • Ono, K., Hasegawa, K., Naiki, H., and Yamada, M. (2004) Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. J. Neurosci. Res. 75, 742-750
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 18
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein, W. L., Krafft, G. A., and Finch, C. E. (2001) Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24, 219-224
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 19
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen, F. E., and Kelly, J. W. (2003) Therapeutic approaches to protein-misfolding diseases. Nature (London) 426, 905-909
    • (2003) Nature (London) , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 20
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening
    • Chang, L., Bakhos, L., Wang, Z., Venton, D. L., and Klein, W. L. (2003) Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening. J. Mol. Neurosci. 20, 305-313
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 305-313
    • Chang, L.1    Bakhos, L.2    Wang, Z.3    Venton, D.L.4    Klein, W.L.5
  • 22
    • 0035349804 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's disease beta-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy
    • De Felice, F. G., Houzel, J. C., Garcia-Abreu, J., Louzada, P. R., Jr., Afonso, R. C., Meirelles, M. N., Lent, R., Neto, V. M., and Ferreira, S. T. (2001) Inhibition of Alzheimer's disease beta-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy. FASEB J. 15, 1297-1299
    • (2001) FASEB J. , vol.15 , pp. 1297-1299
    • De Felice, F.G.1    Houzel, J.C.2    Garcia-Abreu, J.3    Louzada Jr., P.R.4    Afonso, R.C.5    Meirelles, M.N.6    Lent, R.7    Neto, V.M.8    Ferreira, S.T.9
  • 23
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77-83
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 25
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., and Katzman, R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 26
  • 29
    • 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
    • Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., and Klein, W. L. (2003) 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, 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.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 30
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haass, C., Seubert, P., Koo, E. H., and Selkoe, D. J. (1997) Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272, 7977-7982
    • (1997) J. Biol. Chem. , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haass, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 31
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature (London) 416, 535-539
    • (2002) Nature (London) , 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
  • 32
    • 0035807829 scopus 로고    scopus 로고
    • Specific spatial learning deficits become severe with age in beta-amyloid precursor protein transgenic mice that harbor diffuse beta-amyloid deposits but do not form plaques
    • Koistinaho, M., Ort, M., Cimadevilla, J. M., Vondrous, R., Cordell, B., Koistinaho, J., Bures, J., and Higgins, L. S. (2001) Specific spatial learning deficits become severe with age in beta-amyloid precursor protein transgenic mice that harbor diffuse beta-amyloid deposits but do not form plaques. Proc. Natl. Acad. Sci. USA 98, 14675-14680
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14675-14680
    • Koistinaho, M.1    Ort, M.2    Cimadevilla, J.M.3    Vondrous, R.4    Cordell, B.5    Koistinaho, J.6    Bures, J.7    Higgins, L.S.8
  • 39
    • 0036127580 scopus 로고    scopus 로고
    • Set back to Alzheimer vaccine studies
    • Birmingham, K., and Frantz, S. (2002) Set back to Alzheimer vaccine studies. Nat. Med. 8, 199-200
    • (2002) Nat. Med. , vol.8 , pp. 199-200
    • Birmingham, K.1    Frantz, S.2
  • 41
    • 0036544598 scopus 로고    scopus 로고
    • Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization
    • Raghu, P., Reddy, G. B., and Sivakumar, B. (2002) Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization. Arch. Biochem. Biophys. 400, 43-47
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 43-47
    • Raghu, P.1    Reddy, G.B.2    Sivakumar, B.3
  • 42
    • 0038375018 scopus 로고    scopus 로고
    • 4′-Iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters
    • Cardoso, I., Merlini, G., and Saraiva, M. J. (2003) 4′-Iodo- 4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters. FASEB J. 17, 803-809
    • (2003) FASEB J. , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 44
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening
    • Chang, L., Bakhos, L., Wang, Z., Venton, D. L., and Klein, W. L. (2003) Femtomole immunodetection of synthetic and endogenous amyloid-beta oligomers and its application to Alzheimer's disease drug candidate screening. J. Mol. Neurosci. 20, 305-314
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 305-314
    • Chang, L.1    Bakhos, L.2    Wang, Z.3    Venton, D.L.4    Klein, W.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.