메뉴 건너뛰기




Volumn 15, Issue 6, 2009, Pages 637-658

Multivalent & multifunctional ligands to β-amyloid

Author keywords

amyloid; A ; AD drug; Alzheimer's disease; Early diagnosis; Imaging probe; Ligand; Multifunction; Multivalent

Indexed keywords

ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; ANTIOXIDANT; BAPINEUZUMAB; BENZOTHIAZOLE DERIVATIVE; BISPYRIDINIUM DERIVATIVE; CHOLINESTERASE INHIBITOR; CONGO RED; DENDRIMER; DONEPEZIL; FERULIC ACID; GALANTAMINE; HOMOTAURINE; MEMANTINE; METAL CHELATE; N METHYL N BENZYLAMINE; NAPROXEN; NONSTEROID ANTIINFLAMMATORY AGENT; PENTETIC ACID; PHENAZOPYRIDINE; PLACEBO; POLYPHENOL DERIVATIVE; QUINONE DERIVATIVE; RIVASTIGMINE; SKF 64346; TACRINE; THIOFLAVINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VITAMIN; XH 1; LIGAND;

EID: 65549161050     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209787315648     Document Type: Review
Times cited : (29)

References (191)
  • 1
    • 40649091389 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Maslow K. 2008 Alzheimer's disease facts and figures. Alzheimer's Dementia 2008; 4: 110-33.
    • (2008) Alzheimer's Dementia 2008 , vol.4 , pp. 110-133
    • Maslow, K.1
  • 2
    • 0026176163 scopus 로고
    • A contribution concerning the pathological anatomy of mental disturbances in old age, 1899
    • Alzheimer A. A contribution concerning the pathological anatomy of mental disturbances in old age, 1899. Alzheimer Dis Assoc Disord 1991; 5: 69-70.
    • (1991) Alzheimer Dis Assoc Disord , vol.5 , pp. 69-70
    • Alzheimer, A.1
  • 3
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: The amyloid cascade hypothesis. Science 1992; 256: 184-5.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 4
    • 0029147583 scopus 로고
    • Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors
    • Lee RK, Wurtman RJ, Cox AJ, Nitsch RM. Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors. Proc Natl Acad Sci USA 1995; 92: 8083-7.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8083-8087
    • Lee, R.K.1    Wurtman, R.J.2    Cox, A.J.3    Nitsch, R.M.4
  • 5
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486-9.
    • (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
  • 7
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of A beta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher AE, Chaney MO, Kuo YM, Webster SD, Stine WB, Haverkamp LJ, et al. Morphology and toxicity of A beta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J Biol Chem 1996; 271: 20631-5.
    • (1996) J Biol Chem , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5    Haverkamp, L.J.6
  • 8
    • 0031445940 scopus 로고    scopus 로고
    • Mechanism and prevention of neurotoxicity caused by beta-amyloid peptides: Relation to Alzheimer's disease
    • Blanchard BJ, Konopka G, Russell M, Ingram VM. Mechanism and prevention of neurotoxicity caused by beta-amyloid peptides: Relation to Alzheimer's disease. Brain Res 1997; 776: 40-50.
    • (1997) Brain Res , vol.776 , pp. 40-50
    • Blanchard, B.J.1    Konopka, G.2    Russell, M.3    Ingram, V.M.4
  • 9
    • 17344394478 scopus 로고    scopus 로고
    • Age-related amyloid beta protein accumulation induces cellular death and macrophage activation in transgenic mice
    • Shoji M, Kawarabayashi T, Sato M, Sasaki A, Saido TC, Matsubara E, et al. Age-related amyloid beta protein accumulation induces cellular death and macrophage activation in transgenic mice. J Pathol 2000; 191: 93-101.
    • (2000) J Pathol , vol.191 , pp. 93-101
    • Shoji, M.1    Kawarabayashi, T.2    Sato, M.3    Sasaki, A.4    Saido, T.C.5    Matsubara, E.6
  • 10
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • Selkoe DJ, Schenk D. Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol 2003; 43: 545-84.
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 11
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides
    • Hartmann T, Bieger SC, Bruhl B, Tienari PJ, Ida N, Allsop D, et al. Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nat Med 1997; 3: 1016-20.
    • (1997) Nat Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Bruhl, B.3    Tienari, P.J.4    Ida, N.5    Allsop, D.6
  • 12
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • Pitschke M, Prior R, Haupt M, Riesner D. Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nat Med 1998; 4: 832-4.
    • (1998) Nat Med , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 13
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein WL, Stine WB, Jr., Teplow DB. Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 2004; 25: 569-80.
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 14
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine WB, Jr., Dahlgren KN, Krafft GA, LaDu MJ. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem 2003; 278: 11612-22.
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 15
    • 0031891742 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid peptide: Affinity for metal chelates
    • Balakrishnan R, Parthasarathy R, Sulkowski E. Alzheimer's beta-amyloid peptide: Affinity for metal chelates. J Pept Res 1998; 51: 91-5.
    • (1998) J Pept Res , vol.51 , pp. 91-95
    • Balakrishnan, R.1    Parthasarathy, R.2    Sulkowski, E.3
  • 16
    • 0035997233 scopus 로고    scopus 로고
    • Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42
    • Butterfield DA, Kanski J. Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide 1-42. Peptides 2002; 23: 1299-309.
    • (2002) Peptides , vol.23 , pp. 1299-1309
    • Butterfield, D.A.1    Kanski, J.2
  • 17
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease
    • Liu ST, Howlett G, Barrow CJ. Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease. Biochemistry 1999; 38: 9373-8.
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 18
    • 0038676610 scopus 로고    scopus 로고
    • Free radical reactions of methionine in peptides: Mechanisms relevant to beta-amyloid oxidation and Alzheimer's disease
    • Schoneich C, Pogocki D, Hug GL, Bobrowski K. Free radical reactions of methionine in peptides: Mechanisms relevant to beta-amyloid oxidation and Alzheimer's disease. J Am Chem Soc 2003; 125: 13700-13.
    • (2003) J Am Chem Soc , vol.125 , pp. 13700-13713
    • Schoneich, C.1    Pogocki, D.2    Hug, G.L.3    Bobrowski, K.4
  • 19
    • 0028076051 scopus 로고
    • Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease
    • Klunk WE, Debnath ML, Pettegrew JW. Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease. Neurobiol Aging 1994; 15: 691-8.
    • (1994) Neurobiol Aging , vol.15 , pp. 691-698
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 21
    • 0345415139 scopus 로고    scopus 로고
    • 2-Dialkylamino-6-acylmalononitrile substituted naphthalenes (DDNP analogs): Novel diagnostic and therapeutic tools in Alzheimer's disease
    • Agdeppa ED, Kepe V, Liu J, Small GW, Huang SC, Petric A, et al. 2-Dialkylamino-6-acylmalononitrile substituted naphthalenes (DDNP analogs): Novel diagnostic and therapeutic tools in Alzheimer's disease. Mol Imaging Biol 2003; 5: 404-17.
    • (2003) Mol Imaging Biol , vol.5 , pp. 404-417
    • Agdeppa, E.D.1    Kepe, V.2    Liu, J.3    Small, G.W.4    Huang, S.C.5    Petric, A.6
  • 24
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002; 297: 353-6.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 25
    • 33744465230 scopus 로고    scopus 로고
    • PKCepsilon increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice
    • Choi DS, Wang D, Yu GQ, Zhu G, Kharazia VN, Paredes JP, et al. PKCepsilon increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice. Proc Natl Acad Sci USA 2006; 103: 8215-20.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8215-8220
    • Choi, D.S.1    Wang, D.2    Yu, G.Q.3    Zhu, G.4    Kharazia, V.N.5    Paredes, J.P.6
  • 26
    • 33746649088 scopus 로고    scopus 로고
    • Anti-amyloidogenic therapies: Strategies for prevention and treatment of Alzheimer's disease
    • Hamaguchi T, Ono K, Yamada M. Anti-amyloidogenic therapies: Strategies for prevention and treatment of Alzheimer's disease. Cell Mol Life Sci 2006; 63: 1538-52.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1538-1552
    • Hamaguchi, T.1    Ono, K.2    Yamada, M.3
  • 27
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999; 400: 173-7.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 28
    • 33847133125 scopus 로고    scopus 로고
    • Targeting soluble Abeta peptide with Tramiprosate for the treatment of brain amyloidosis
    • Gervais F, Paquette J, Morissette C, Krzywkowski P, Yu M, Azzi M, et al. Targeting soluble Abeta peptide with Tramiprosate for the treatment of brain amyloidosis. Neurobiol Aging 2007; 28: 537-47.
    • (2007) Neurobiol Aging , vol.28 , pp. 537-547
    • Gervais, F.1    Paquette, J.2    Morissette, C.3    Krzywkowski, P.4    Yu, M.5    Azzi, M.6
  • 29
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, Gray DN, Jones WD, McLean CA, et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 2001; 30: 665-76.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5    McLean, C.A.6
  • 30
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimer's disease
    • Melnikova I. Therapies for Alzheimer's disease. Nat Rev Drug Discov 2007; 6: 341-2.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 341-342
    • Melnikova, I.1
  • 31
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen M, Choi SK, Whitesides GM. Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors. Angew Chem Int Ed 1998; 37: 2755-94.
    • (1998) Angew Chem Int Ed , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 33
    • 33746862160 scopus 로고    scopus 로고
    • The physicochemical challenges of designing multiple ligands
    • Morphy R, Rankovic Z. The physicochemical challenges of designing multiple ligands. J Med Chem 2006; 49: 4961-70.
    • (2006) J Med Chem , vol.49 , pp. 4961-4970
    • Morphy, R.1    Rankovic, Z.2
  • 35
    • 27144449695 scopus 로고    scopus 로고
    • Designed multiple ligands. An emerging drug discovery paradigm
    • Morphy R, Rankovic Z. Designed multiple ligands. An emerging drug discovery paradigm. J Med Chem 2005; 48: 6523-43.
    • (2005) J Med Chem , vol.48 , pp. 6523-6543
    • Morphy, R.1    Rankovic, Z.2
  • 36
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk WE, Pettegrew JW, Abraham DJ. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 1989; 37: 1273-81.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 37
    • 0032849874 scopus 로고    scopus 로고
    • LeVine H, 3rd. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 1999; 309: 274-84.
    • LeVine H, 3rd. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 1999; 309: 274-84.
  • 38
    • 0029083059 scopus 로고
    • Chrysamine-G binding to Alzheimer and control brain: Autopsy study of a new amyloid probe
    • Klunk WE, Debnath ML, Pettegrew JW. Chrysamine-G binding to Alzheimer and control brain: Autopsy study of a new amyloid probe. Neurobiol Aging 1995; 16: 541-8.
    • (1995) Neurobiol Aging , vol.16 , pp. 541-548
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 39
    • 0015596655 scopus 로고
    • Screening for neurofibrillary tangles and argyrophilic plaques with Congo Red and polarized light
    • Stokes MI, Trickey RJ. Screening for neurofibrillary tangles and argyrophilic plaques with Congo Red and polarized light. J Clin Pathol 1973; 26: 241-2.
    • (1973) J Clin Pathol , vol.26 , pp. 241-242
    • Stokes, M.I.1    Trickey, R.J.2
  • 40
    • 0031060245 scopus 로고    scopus 로고
    • Relationship between immobilised artificial membrane chromatographic retention and the brain penetration of structurally diverse drugs
    • Salminen T, Pulli A, Taskinen J. Relationship between immobilised artificial membrane chromatographic retention and the brain penetration of structurally diverse drugs. J Pharm Biomed Anal 1997; 15: 469-77
    • (1997) J Pharm Biomed Anal , vol.15 , pp. 469-477
    • Salminen, T.1    Pulli, A.2    Taskinen, J.3
  • 41
    • 0035811461 scopus 로고    scopus 로고
    • Isomerization of (Z,Z) to (E,E)1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene in strong base: Probes for amyloid plaques in the brain
    • Lee CW, Zhuang ZP, Kung MP, Plossl K, Skovronsky D, Gur T, et al. Isomerization of (Z,Z) to (E,E)1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene in strong base: Probes for amyloid plaques in the brain. J Med Chem 2001; 44: 2270-5.
    • (2001) J Med Chem , vol.44 , pp. 2270-2275
    • Lee, C.W.1    Zhuang, Z.P.2    Kung, M.P.3    Plossl, K.4    Skovronsky, D.5    Gur, T.6
  • 42
    • 0036676012 scopus 로고    scopus 로고
    • Radioiodinated styrylbenzene derivatives as potential SPECT imaging agents for amyloid plaque detection in Alzheimer's disease
    • Kung MP, Hou C, Zhuang ZP, Skovronsky DM, Zhang B, Gur TL, et al. Radioiodinated styrylbenzene derivatives as potential SPECT imaging agents for amyloid plaque detection in Alzheimer's disease. J Mol Neurosci 2002; 19: 7-10.
    • (2002) J Mol Neurosci , vol.19 , pp. 7-10
    • Kung, M.P.1    Hou, C.2    Zhuang, Z.P.3    Skovronsky, D.M.4    Zhang, B.5    Gur, T.L.6
  • 43
    • 0035159024 scopus 로고    scopus 로고
    • IBOX(2-(4′-dimethylaminophenyl)-6-iodobenzoxazole): A ligand for imaging amyloid plaques in the brain
    • Zhuang ZP, Kung MP, Hou C, Plossl K, Skovronsky D, Gur TL, et al. IBOX(2-(4′-dimethylaminophenyl)-6-iodobenzoxazole): A ligand for imaging amyloid plaques in the brain. Nucl Med Biol 2001; 28: 887-94
    • (2001) Nucl Med Biol , vol.28 , pp. 887-894
    • Zhuang, Z.P.1    Kung, M.P.2    Hou, C.3    Plossl, K.4    Skovronsky, D.5    Gur, T.L.6
  • 44
    • 0142075238 scopus 로고    scopus 로고
    • 11C-labeled stilbene derivatives as Abeta-aggregate-specific PET imaging agents for Alzheimer's disease
    • Ono M, Wilson A, Nobrega J, Westaway D, Verhoeff P, Zhuang ZP, et al. 11C-labeled stilbene derivatives as Abeta-aggregate-specific PET imaging agents for Alzheimer's disease. Nucl Med Biol 2003; 30: 565-71.
    • (2003) Nucl Med Biol , vol.30 , pp. 565-571
    • Ono, M.1    Wilson, A.2    Nobrega, J.3    Westaway, D.4    Verhoeff, P.5    Zhuang, Z.P.6
  • 46
    • 0037195577 scopus 로고    scopus 로고
    • IMPY: An improved thioflavin-T derivative for in vivo labeling of beta-amyloid plaques
    • Kung MP, Hou C, Zhuang ZP, Zhang B, Skovronsky D, Trojanowski JQ, et al. IMPY: An improved thioflavin-T derivative for in vivo labeling of beta-amyloid plaques. Brain Res 2002; 956: 202-10.
    • (2002) Brain Res , vol.956 , pp. 202-210
    • Kung, M.P.1    Hou, C.2    Zhuang, Z.P.3    Zhang, B.4    Skovronsky, D.5    Trojanowski, J.Q.6
  • 47
    • 2342446265 scopus 로고    scopus 로고
    • Imaging beta-amyloid plaques and neurofibrillary tangles in the aging human brain
    • Mathis CA, Wang Y, Klunk WE. Imaging beta-amyloid plaques and neurofibrillary tangles in the aging human brain. Curr Pharm Des 2004; 10: 1469-92.
    • (2004) Curr Pharm Des , vol.10 , pp. 1469-1492
    • Mathis, C.A.1    Wang, Y.2    Klunk, W.E.3
  • 48
    • 39049114657 scopus 로고    scopus 로고
    • Synthesis and evaluation of stilbenylbenzoxazole and stilbenylbenzothiazole derivatives for detecting beta-amyloid fibrils
    • Lee JH, Byeon SR, Lim SJ, Oh SJ, Moon DH, Yoo KH, et al. Synthesis and evaluation of stilbenylbenzoxazole and stilbenylbenzothiazole derivatives for detecting beta-amyloid fibrils. Bioorg Med Chem Lett 2008; 18: 1534-7.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 1534-1537
    • Lee, J.H.1    Byeon, S.R.2    Lim, S.J.3    Oh, S.J.4    Moon, D.H.5    Yoo, K.H.6
  • 49
    • 40149109194 scopus 로고    scopus 로고
    • Isoindol-1,3-dione and isoindol-1-one derivatives with high binding affinity to beta-amyloid fibrils
    • Lee HJ, Lim SJ, Oh SJ, Moon DH, Kim DJ, Tae J, et al. Isoindol-1,3-dione and isoindol-1-one derivatives with high binding affinity to beta-amyloid fibrils. Bioorg Med Chem Lett 2008; 18: 1628-31.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 1628-1631
    • Lee, H.J.1    Lim, S.J.2    Oh, S.J.3    Moon, D.H.4    Kim, D.J.5    Tae, J.6
  • 50
    • 57349127526 scopus 로고    scopus 로고
    • Tramiprosate falls short in phase III Alzheimer's trial
    • 35
    • Sullivan M. Tramiprosate falls short in phase III Alzheimer's trial. Clin Psychiatry News 2007; 35: 27.
    • (2007) Clin Psychiatry News , pp. 27
    • Sullivan, M.1
  • 52
    • 33748767945 scopus 로고    scopus 로고
    • Amyloid-{beta} peptide remnants in AN-1792-immunized Alzheimer's disease patients: A biochemical analysis
    • Patton RL, Kalback WM, Esh CL, Kokjohn TA, Van Vickle GD, Luehrs DC, et al. Amyloid-{beta} peptide remnants in AN-1792-immunized Alzheimer's disease patients: A biochemical analysis. Am J Pathol 2006; 169: 1048-63.
    • (2006) Am J Pathol , vol.169 , pp. 1048-1063
    • Patton, R.L.1    Kalback, W.M.2    Esh, C.L.3    Kokjohn, T.A.4    Van Vickle, G.D.5    Luehrs, D.C.6
  • 53
    • 0036848056 scopus 로고    scopus 로고
    • A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro
    • Nakagami Y, Nishimura S, Murasugi T, Kaneko I, Meguro M, Marumoto S, et al. A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro. Br J Pharmacol 2002; 137: 676-82.
    • (2002) Br J Pharmacol , vol.137 , pp. 676-682
    • Nakagami, Y.1    Nishimura, S.2    Murasugi, T.3    Kaneko, I.4    Meguro, M.5    Marumoto, S.6
  • 54
    • 0031873102 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto C, Sigurdsson EM, Morelli L, Kumar RA, Castano EM, Frangione B. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat Med 1998; 4: 822-6.
    • (1998) Nat Med , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 56
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem Biophys Res Commun 1996; 226: 672-80.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 57
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J Mol Biol 1992; 228: 460-73.
    • (1992) J Mol Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 59
    • 0036289548 scopus 로고    scopus 로고
    • Inhibitors of fibril formation and cytotoxicity of beta-amyloid peptide composed of KLVFF recognition element and flexible hydrophilic disrupting element
    • Watanabe K, Nakamura K, Akikusa S, Okada T, Kodaka M, Konakahara T, et al. Inhibitors of fibril formation and cytotoxicity of beta-amyloid peptide composed of KLVFF recognition element and flexible hydrophilic disrupting element. Biochem Biophys Res Commun 2002; 290: 121-4.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 121-124
    • Watanabe, K.1    Nakamura, K.2    Akikusa, S.3    Okada, T.4    Kodaka, M.5    Konakahara, T.6
  • 60
    • 6044240725 scopus 로고    scopus 로고
    • Beta-sheet breaker peptide prevents Abeta-induced spatial memory impairments with partial reduction of amyloid deposits
    • Chacon MA, Barria MI, Soto C, Inestrosa NC. Beta-sheet breaker peptide prevents Abeta-induced spatial memory impairments with partial reduction of amyloid deposits. Mol Psychiatry 2004; 9: 953-61.
    • (2004) Mol Psychiatry , vol.9 , pp. 953-961
    • Chacon, M.A.1    Barria, M.I.2    Soto, C.3    Inestrosa, N.C.4
  • 61
    • 35348934391 scopus 로고    scopus 로고
    • Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation
    • Chafekar SM, Malda H, Merkx M, Meijer EW, Viertl D, Lashuel HA, et al. Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation. ChemBioChem 2007; 8: 1857-64.
    • (2007) ChemBioChem , vol.8 , pp. 1857-1864
    • Chafekar, S.M.1    Malda, H.2    Merkx, M.3    Meijer, E.W.4    Viertl, D.5    Lashuel, H.A.6
  • 62
    • 33747616201 scopus 로고    scopus 로고
    • Chemistry. Dendrimers at work
    • Helms B, Meijer EW. Chemistry. Dendrimers at work. Science 2006; 313: 929-30.
    • (2006) Science , vol.313 , pp. 929-930
    • Helms, B.1    Meijer, E.W.2
  • 64
    • 12244305529 scopus 로고    scopus 로고
    • Multiple-peptide conjugates for binding beta-amyloid plaques of Alzheimer's disease
    • Zhang G, Leibowitz MJ, Sinko PJ, Stein S. Multiple-peptide conjugates for binding beta-amyloid plaques of Alzheimer's disease. Bioconjug Chem 2003; 14: 86-92.
    • (2003) Bioconjug Chem , vol.14 , pp. 86-92
    • Zhang, G.1    Leibowitz, M.J.2    Sinko, P.J.3    Stein, S.4
  • 66
    • 44049085833 scopus 로고    scopus 로고
    • A multimeric quinacrine conjugate as a potential inhibitor of Alzheimer's beta-amyloid fibril formation
    • Dolphin GT, Chierici S, Ouberai M, Dumy P, Garcia J. A multimeric quinacrine conjugate as a potential inhibitor of Alzheimer's beta-amyloid fibril formation. ChemBioChem 2008; 9: 952-63.
    • (2008) ChemBioChem , vol.9 , pp. 952-963
    • Dolphin, G.T.1    Chierici, S.2    Ouberai, M.3    Dumy, P.4    Garcia, J.5
  • 68
    • 33746216304 scopus 로고    scopus 로고
    • Control of amyloid beta-peptide protofibril formation by a designed template assembly. Angew
    • Dolphin GT, Dumy P, Garcia J. Control of amyloid beta-peptide protofibril formation by a designed template assembly. Angew Chem Int Ed 2006; 45: 2699-702.
    • (2006) Chem Int Ed , vol.45 , pp. 2699-2702
    • Dolphin, G.T.1    Dumy, P.2    Garcia, J.3
  • 69
    • 0024039077 scopus 로고
    • Nature's rules and chemist's tools: A way for creating novel proteins
    • Mutter M. Nature's rules and chemist's tools: A way for creating novel proteins. Trends Biochem Sci 1988; 13: 260-5.
    • (1988) Trends Biochem Sci , vol.13 , pp. 260-265
    • Mutter, M.1
  • 70
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT, Jr. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-8.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 72
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • Naiki H, Gejyo F. Kinetic analysis of amyloid fibril formation. Methods Enzymol 1999; 309: 305-18.
    • (1999) Methods Enzymol , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 73
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro
    • Naiki H, Nakakuki K. First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. Lab Invest 1996; 74: 374-83.
    • (1996) Lab Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 74
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-beta efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DeMattos RB, Bales KR, Cummins DJ, Paul SM, Holtzman DM. Brain to plasma amyloid-beta efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science 2002; 295: 2264-7.
    • (2002) Science , vol.295 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 75
    • 0034986151 scopus 로고    scopus 로고
    • Protection against beta-amyloid peptide toxicity in vivo with long-term administration of ferulic acid
    • Yan JJ, Cho JY, Kim HS, Kim KL, Jung JS, Huh SO, et al. Protection against beta-amyloid peptide toxicity in vivo with long-term administration of ferulic acid. Br J Pharmacol 2001; 133: 89-96.
    • (2001) Br J Pharmacol , vol.133 , pp. 89-96
    • Yan, J.J.1    Cho, J.Y.2    Kim, H.S.3    Kim, K.L.4    Jung, J.S.5    Huh, S.O.6
  • 76
    • 13744252140 scopus 로고    scopus 로고
    • A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by beta-amyloid (1-42)
    • Lee KH, Shin BH, Shin KJ, Kim DJ, Yu J. A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by beta-amyloid (1-42). Biochem Biophys Res Commun 2005; 328: 816-23.
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 816-823
    • Lee, K.H.1    Shin, B.H.2    Shin, K.J.3    Kim, D.J.4    Yu, J.5
  • 77
    • 33846931387 scopus 로고    scopus 로고
    • Bis-styrylpyridine and bis-styrylbenzene derivatives as inhibitors for Abeta fibril formation
    • Byeon SR, Lee JH, Sohn JH, Kim DC, Shin KJ, Yoo KH, et al. Bis-styrylpyridine and bis-styrylbenzene derivatives as inhibitors for Abeta fibril formation. Bioorg Med Chem Lett 2007; 17: 1466-70.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 1466-1470
    • Byeon, S.R.1    Lee, J.H.2    Sohn, J.H.3    Kim, D.C.4    Shin, K.J.5    Yoo, K.H.6
  • 79
    • 34250674908 scopus 로고    scopus 로고
    • Ferulic acid and benzothiazole dimer derivatives with high binding affinity to beta-amyloid fibrils
    • Byeon SR, Jin YJ, Lim SJ, Lee JH, Yoo KH, Shin KJ, et al. Ferulic acid and benzothiazole dimer derivatives with high binding affinity to beta-amyloid fibrils. Bioorg Med Chem Lett 2007; 17: 4022-5.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 4022-4025
    • Byeon, S.R.1    Jin, Y.J.2    Lim, S.J.3    Lee, J.H.4    Yoo, K.H.5    Shin, K.J.6
  • 80
    • 0038792263 scopus 로고    scopus 로고
    • Synthesis and evaluation of 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents
    • Mathis CA, Wang Y, Holt DP, Huang GF, Debnath ML, Klunk WE. Synthesis and evaluation of 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents. J Med Chem 2003; 46: 2740-54.
    • (2003) J Med Chem , vol.46 , pp. 2740-2754
    • Mathis, C.A.1    Wang, Y.2    Holt, D.P.3    Huang, G.F.4    Debnath, M.L.5    Klunk, W.E.6
  • 81
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486-9.
    • (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
  • 82
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation
    • Soreghan B, Kosmoski J, Glabe C. Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation. J Biol Chem 1994; 269: 28551-4.
    • (1994) J Biol Chem , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 83
    • 0034725656 scopus 로고    scopus 로고
    • A conformation change in the carboxyl terminus of Alzheimer's Abeta (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis
    • Garzon-Rodriguez W, Vega A, Sepulveda-Becerra M, Milton S, Johnson DA, Yatsimirsky AK, et al. A conformation change in the carboxyl terminus of Alzheimer's Abeta (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis. J Biol Chem 2000; 275: 22645-9.
    • (2000) J Biol Chem , vol.275 , pp. 22645-22649
    • Garzon-Rodriguez, W.1    Vega, A.2    Sepulveda-Becerra, M.3    Milton, S.4    Johnson, D.A.5    Yatsimirsky, A.K.6
  • 86
    • 33947546504 scopus 로고    scopus 로고
    • Implications of co-morbidity for etiology and treatment of neurodegenerative diseases with multifunctional neuroprotectiveneurorescue drugs; ladostigil
    • Youdim MB, Amit T, Bar-Am O, Weinreb O, Yogev-Falach M. Implications of co-morbidity for etiology and treatment of neurodegenerative diseases with multifunctional neuroprotectiveneurorescue drugs; ladostigil. Neurotox Res 2006; 10: 181-92.
    • (2006) Neurotox Res , vol.10 , pp. 181-192
    • Youdim, M.B.1    Amit, T.2    Bar-Am, O.3    Weinreb, O.4    Yogev-Falach, M.5
  • 87
    • 0035856813 scopus 로고    scopus 로고
    • Ramanathan S, Qiu B, Pooyan S, Zhang G, Stein S, Leibowitz MJ, et al. Targeted PEG-based bioconjugates enhance the cellular uptake and transport of a HIV-1 TAT nonapeptide. J Control Release 2001; 77: 199-212
    • Ramanathan S, Qiu B, Pooyan S, Zhang G, Stein S, Leibowitz MJ, et al. Targeted PEG-based bioconjugates enhance the cellular uptake and transport of a HIV-1 TAT nonapeptide. J Control Release 2001; 77: 199-212.
  • 88
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA. Convergent solutions to binding at a protein-protein interface. Science 2000; 287: 1279-83.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 91
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation
    • Gestwicki JE, Crabtree GR, Graef IA. Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation. Science 2004; 306: 865-9.
    • (2004) Science , vol.306 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 92
    • 0001019593 scopus 로고
    • Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12
    • Holt DA, Luengo JI, Yamashita DS, Oh HJ, Konialian AL, Yen HK, et al. Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12. J Am Chem Soc 1993; 115: 9925-38.
    • (1993) J Am Chem Soc , vol.115 , pp. 9925-9938
    • Holt, D.A.1    Luengo, J.I.2    Yamashita, D.S.3    Oh, H.J.4    Konialian, A.L.5    Yen, H.K.6
  • 94
    • 0036860355 scopus 로고    scopus 로고
    • Amyloid binding ligands as Alzheimer's disease therapies
    • Lee VM. Amyloid binding ligands as Alzheimer's disease therapies. Neurobiol Aging 2002; 23: 1039-42.
    • (2002) Neurobiol Aging , vol.23 , pp. 1039-1042
    • Lee, V.M.1
  • 95
    • 0034718206 scopus 로고    scopus 로고
    • Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization
    • Findeis MA. Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization. Biochim Biophys Acta 2000; 1502: 76-84.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 76-84
    • Findeis, M.A.1
  • 96
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CS, Moir RD, Huang X, Scarpa RC, Bacarra NM, Romano DM, et al. Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 1998; 273: 12817-26.
    • (1998) J Biol Chem , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.3    Scarpa, R.C.4    Bacarra, N.M.5    Romano, D.M.6
  • 97
    • 0027980901 scopus 로고    scopus 로고
    • Bush AI, Pettingell WH, Multhaup G, d Paradis M, Vonsattel JP, Gusella JF, et al. Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 1994; 265: 1464-7.
    • Bush AI, Pettingell WH, Multhaup G, d Paradis M, Vonsattel JP, Gusella JF, et al. Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 1994; 265: 1464-7.
  • 98
  • 99
    • 27744456516 scopus 로고    scopus 로고
    • Preparation of cyclo-phen-type ligands: Chelators of metal ions as potential therapeutic agents in the treatment of neurodegenerative diseases
    • Boldron C, Van der Auwera I, Deraeve C, Gornitzka H, Wera S, Pitie M, et al. Preparation of cyclo-phen-type ligands: Chelators of metal ions as potential therapeutic agents in the treatment of neurodegenerative diseases. ChemBioChem 2005; 6: 1976-80.
    • (2005) ChemBioChem , vol.6 , pp. 1976-1980
    • Boldron, C.1    Van der Auwera, I.2    Deraeve, C.3    Gornitzka, H.4    Wera, S.5    Pitie, M.6
  • 100
    • 0033551782 scopus 로고    scopus 로고
    • Aqueous dissolution of Alzheimer's disease Abeta amyloid deposits by biometal depletion
    • Cherny RA, Legg JT, McLean CA, Fairlie DP, Huang X, Atwood CS, et al. Aqueous dissolution of Alzheimer's disease Abeta amyloid deposits by biometal depletion. J Biol Chem 1999; 274: 23223-8.
    • (1999) J Biol Chem , vol.274 , pp. 23223-23228
    • Cherny, R.A.1    Legg, J.T.2    McLean, C.A.3    Fairlie, D.P.4    Huang, X.5    Atwood, C.S.6
  • 101
    • 12344251715 scopus 로고    scopus 로고
    • Novel D-penicillamine carrying nanoparticles for metal chelation therapy in Alzheimer's and other CNS diseases
    • Cui Z, Lockman PR, Atwood CS, Hsu CH, Gupte A, Allen DD, et al. Novel D-penicillamine carrying nanoparticles for metal chelation therapy in Alzheimer's and other CNS diseases. Eur J Pharm Biopharm 2005; 59: 263-72.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 263-272
    • Cui, Z.1    Lockman, P.R.2    Atwood, C.S.3    Hsu, C.H.4    Gupte, A.5    Allen, D.D.6
  • 103
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: A pilot phase 2 clinical trial
    • Ritchie CW, Bush AI, Mackinnon A, Macfarlane S, Mastwyk M, MacGregor L, et al. Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: A pilot phase 2 clinical trial. Arch Neurol 2003; 60: 1685-91.
    • (2003) Arch Neurol , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1    Bush, A.I.2    Mackinnon, A.3    Macfarlane, S.4    Mastwyk, M.5    MacGregor, L.6
  • 104
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann
    • Huang X, Moir RD, Tanzi RE, Bush AI, Rogers JT. Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann N Y Acad Sci 2004; 1012: 153-63.
    • (2004) N Y Acad Sci , vol.1012 , pp. 153-163
    • Huang, X.1    Moir, R.D.2    Tanzi, R.E.3    Bush, A.I.4    Rogers, J.T.5
  • 105
    • 9744219638 scopus 로고    scopus 로고
    • Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis
    • Dedeoglu A, Cormier K, Payton S, Tseitlin KA, Kremsky JN, Lai L, et al. Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis. Exp Gerontol 2004; 39: 1641-9
    • (2004) Exp Gerontol , vol.39 , pp. 1641-1649
    • Dedeoglu, A.1    Cormier, K.2    Payton, S.3    Tseitlin, K.A.4    Kremsky, J.N.5    Lai, L.6
  • 106
    • 34848913126 scopus 로고    scopus 로고
    • Cleavage agents for soluble oligomers of amyloid beta peptides. Angew
    • Suh J, Yoo SH, Kim MG, Jeong K, Ahn JY, Kim MS, et al. Cleavage agents for soluble oligomers of amyloid beta peptides. Angew Chem Int Ed 2007; 46: 7064-7.
    • (2007) Chem Int Ed , vol.46 , pp. 7064-7067
    • Suh, J.1    Yoo, S.H.2    Kim, M.G.3    Jeong, K.4    Ahn, J.Y.5    Kim, M.S.6
  • 107
    • 0016401265 scopus 로고
    • Facile intramolecular hydrolysis of dipeptides and glycinamide
    • Buckingham DA, Keene FR, Sargeson AM. Facile intramolecular hydrolysis of dipeptides and glycinamide. J Am Chem Soc 1974; 96: 4981-3.
    • (1974) J Am Chem Soc , vol.96 , pp. 4981-4983
    • Buckingham, D.A.1    Keene, F.R.2    Sargeson, A.M.3
  • 110
    • 0037533955 scopus 로고    scopus 로고
    • Toward protein-cleaving catalytic drugs: Artificial protease selective for myoglobin
    • Jeon JW, Son SJ, Yoo CE, Hong IS, Suh J. Toward protein-cleaving catalytic drugs: Artificial protease selective for myoglobin. Bioorg Med Chem 2003; 11: 2901-10.
    • (2003) Bioorg Med Chem , vol.11 , pp. 2901-2910
    • Jeon, J.W.1    Son, S.J.2    Yoo, C.E.3    Hong, I.S.4    Suh, J.5
  • 111
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue LF, Kuo YM, Roher AE, Brachova L, Shen Y, Sue L, et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol 1999; 155: 853-62.
    • (1999) Am J Pathol , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5    Sue, L.6
  • 112
    • 0011162190 scopus 로고
    • Selective loss of central cholinergic neurons in Alzheimer's disease
    • Davies P, Maloney AJ. Selective loss of central cholinergic neurons in Alzheimer's disease. Lancet 1976; 2: 1403.
    • (1976) Lancet , vol.2 , pp. 1403
    • Davies, P.1    Maloney, A.J.2
  • 113
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus RT, Dean RL, 3rd, Beer B, Lippa AS. The cholinergic hypothesis of geriatric memory dysfunction. Science 1982; 217: 408-14.
    • (1982) Science , vol.217 , pp. 408-414
    • Bartus, R.T.1    Dean 3rd, R.L.2    Beer, B.3    Lippa, A.S.4
  • 115
    • 0036482371 scopus 로고    scopus 로고
    • Cholinergic drugs in pharmacotherapy of Alzheimer's disease
    • Camps P, Muñoz-Torrero D. Cholinergic drugs in pharmacotherapy of Alzheimer's disease. Mini Rev Med Chem 2002; 2: 11-25.
    • (2002) Mini Rev Med Chem , vol.2 , pp. 11-25
    • Camps, P.1    Muñoz-Torrero, D.2
  • 116
    • 0028270519 scopus 로고
    • A 30-week randomized controlled trial of high-dose tacrine in patients with Alzheimer's disease. The Tacrine Study Group
    • Knapp MJ, Knopman DS, Solomon PR, Pendlebury WW, Davis CS, Gracon SI. A 30-week randomized controlled trial of high-dose tacrine in patients with Alzheimer's disease. The Tacrine Study Group. JAMA 1994; 271: 985-91.
    • (1994) JAMA , vol.271 , pp. 985-991
    • Knapp, M.J.1    Knopman, D.S.2    Solomon, P.R.3    Pendlebury, W.W.4    Davis, C.S.5    Gracon, S.I.6
  • 117
    • 0033985927 scopus 로고    scopus 로고
    • Rivastigmine, a new-generation cholinesterase inhibitor for the treatment of Alzheimer's disease
    • Jann MW. Rivastigmine, a new-generation cholinesterase inhibitor for the treatment of Alzheimer's disease. Pharmacotherapy 2000; 20: 1-12.
    • (2000) Pharmacotherapy , vol.20 , pp. 1-12
    • Jann, M.W.1
  • 118
    • 0032507788 scopus 로고    scopus 로고
    • Donepezil improves cognition and global function in Alzheimer disease: A 15-week, double-blind, placebo-controlled study. Donepezil Study Group
    • Rogers SL, Doody RS, Mohs RC, Friedhoff LT. Donepezil improves cognition and global function in Alzheimer disease: A 15-week, double-blind, placebo-controlled study. Donepezil Study Group. Arch Intern Med 1998; 158: 1021-31.
    • (1998) Arch Intern Med , vol.158 , pp. 1021-1031
    • Rogers, S.L.1    Doody, R.S.2    Mohs, R.C.3    Friedhoff, L.T.4
  • 119
    • 0034627263 scopus 로고    scopus 로고
    • Efficacy and safety of galantamine in patients with mild to moderate Alzheimer's disease: Multicentre randomised controlled trial. Galantamine International-1 Study Group
    • Wilcock GK, Lilienfeld S, Gaens E, Addington D, Ancill R, Bergman H, et al. Efficacy and safety of galantamine in patients with mild to moderate Alzheimer's disease: Multicentre randomised controlled trial. Galantamine International-1 Study Group. Br Med J 2000; 321: 1445-9.
    • (2000) Br Med J , vol.321 , pp. 1445-1449
    • Wilcock, G.K.1    Lilienfeld, S.2    Gaens, E.3    Addington, D.4    Ancill, R.5    Bergman, H.6
  • 120
    • 0346656610 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition in Alzheimer's Disease
    • Ibach B, Haen E. Acetylcholinesterase inhibition in Alzheimer's Disease. Curr Pharm Des 2004; 10: 231-51.
    • (2004) Curr Pharm Des , vol.10 , pp. 231-251
    • Ibach, B.1    Haen, E.2
  • 121
    • 0037298750 scopus 로고    scopus 로고
    • beta-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies
    • Bartolini M, Bertucci C, Cavrini V, Andrisano V. beta-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies. Biochem Pharmacol 2003; 65: 407-16.
    • (2003) Biochem Pharmacol , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 122
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, Linker C, et al. Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme. Neuron 1996; 16: 881-91.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6
  • 123
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils
    • Alvarez A, Opazo C, Alarcon R, Garrido J, Inestrosa NC. Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils. J Mol Biol 1997; 272: 348-61.
    • (1997) J Mol Biol , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcon, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 124
    • 0344417185 scopus 로고    scopus 로고
    • Neurotoxicity of acetylcholinesterase amyloid beta-peptide aggregates is dependent on the type of Abeta peptide and the AChE concentration present in the complexes
    • Muñoz FJ, Inestrosa NC. Neurotoxicity of acetylcholinesterase amyloid beta-peptide aggregates is dependent on the type of Abeta peptide and the AChE concentration present in the complexes. FEBS Lett 1999; 450: 205-9.
    • (1999) FEBS Lett , vol.450 , pp. 205-209
    • Muñoz, F.J.1    Inestrosa, N.C.2
  • 125
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation
    • De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry 2001; 40: 10447-57.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 127
    • 0036315026 scopus 로고    scopus 로고
    • Inhibition of acetyl- and butyryl-cholinesterase in the cerebrospinal fluid of patients with Alzheimer's disease by rivastigmine: Correlation with cognitive benefit
    • Giacobini E, Spiegel R, Enz A, Veroff AE, Cutler NR. Inhibition of acetyl- and butyryl-cholinesterase in the cerebrospinal fluid of patients with Alzheimer's disease by rivastigmine: Correlation with cognitive benefit. J Neural Transm 2002; 109: 1053-65.
    • (2002) J Neural Transm , vol.109 , pp. 1053-1065
    • Giacobini, E.1    Spiegel, R.2    Enz, A.3    Veroff, A.E.4    Cutler, N.R.5
  • 128
    • 0035661483 scopus 로고    scopus 로고
    • A new therapeutic target in Alzheimer's disease treatment: Attention to butyrylcholinesterase
    • Greig NH, Utsuki T, Yu Q, Zhu X, Holloway HW, Perry T, et al. A new therapeutic target in Alzheimer's disease treatment: Attention to butyrylcholinesterase. Curr Med Res Opin 2001; 17: 159-65.
    • (2001) Curr Med Res Opin , vol.17 , pp. 159-165
    • Greig, N.H.1    Utsuki, T.2    Yu, Q.3    Zhu, X.4    Holloway, H.W.5    Perry, T.6
  • 130
    • 43949112301 scopus 로고    scopus 로고
    • Benzofuran-based hybrid compounds for the inhibition of cholinesterase activity, beta amyloid aggregation, and abeta neurotoxicity
    • Rizzo S, Riviere C, Piazzi L, Bisi A, Gobbi S, Bartolini M, et al. Benzofuran-based hybrid compounds for the inhibition of cholinesterase activity, beta amyloid aggregation, and abeta neurotoxicity. J Med Chem 2008; 51: 2883-6.
    • (2008) J Med Chem , vol.51 , pp. 2883-2886
    • Rizzo, S.1    Riviere, C.2    Piazzi, L.3    Bisi, A.4    Gobbi, S.5    Bartolini, M.6
  • 132
    • 21244442338 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: Xanthostigmine derivatives blocking the acetylcholinesterase-induced beta-amyloid aggregation
    • Belluti F, Rampa A, Piazzi L, Bisi A, Gobbi S, Bartolini M, et al. Cholinesterase inhibitors: Xanthostigmine derivatives blocking the acetylcholinesterase-induced beta-amyloid aggregation. J Med Chem 2005; 48: 4444-56.
    • (2005) J Med Chem , vol.48 , pp. 4444-4456
    • Belluti, F.1    Rampa, A.2    Piazzi, L.3    Bisi, A.4    Gobbi, S.5    Bartolini, M.6
  • 133
    • 0035829439 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors: SAR and kinetic studies on omega-N-methyl-N-(3-alkylcarbamoyloxyphenyl)methylaminoalkoxyaryl derivatives
    • Rampa A, Piazzi L, Belluti F, Gobbi S, Bisi A, Bartolini M, et al. Acetylcholinesterase inhibitors: SAR and kinetic studies on omega-N-methyl-N-(3-alkylcarbamoyloxyphenyl)methylaminoalkoxyaryl derivatives. J Med Chem 2001; 44: 3810-20.
    • (2001) J Med Chem , vol.44 , pp. 3810-3820
    • Rampa, A.1    Piazzi, L.2    Belluti, F.3    Gobbi, S.4    Bisi, A.5    Bartolini, M.6
  • 135
    • 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, Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. J Neurosci Res 2004; 75: 742-50.
    • (2004) J Neurosci Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 136
    • 28844431542 scopus 로고    scopus 로고
    • Search for dual function inhibitors for Alzheimer's disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Abeta fibril formation inhibition capacity
    • Kapkova P, Alptuzun V, Frey P, Erciyas E, Holzgrabe U. Search for dual function inhibitors for Alzheimer's disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Abeta fibril formation inhibition capacity. Bioorg Med Chem 2006; 14: 472-8.
    • (2006) Bioorg Med Chem , vol.14 , pp. 472-478
    • Kapkova, P.1    Alptuzun, V.2    Frey, P.3    Erciyas, E.4    Holzgrabe, U.5
  • 137
    • 0348108039 scopus 로고    scopus 로고
    • Synthesis, biological activity, and docking studies of new acetylcholinesterase inhibitors of the bispyridinium type
    • Kapkova P, Stiefl N, Surig U, Engels B, Baumann K, Holzgrabe U. Synthesis, biological activity, and docking studies of new acetylcholinesterase inhibitors of the bispyridinium type. Arch Pharm 2003; 336: 523-40.
    • (2003) Arch Pharm , vol.336 , pp. 523-540
    • Kapkova, P.1    Stiefl, N.2    Surig, U.3    Engels, B.4    Baumann, K.5    Holzgrabe, U.6
  • 138
    • 28844462038 scopus 로고    scopus 로고
    • A review of antioxidants and Alzheimer's disease
    • Frank B, Gupta S. A review of antioxidants and Alzheimer's disease. Ann Clin Psychiatry 2005; 17: 269-86.
    • (2005) Ann Clin Psychiatry , vol.17 , pp. 269-286
    • Frank, B.1    Gupta, S.2
  • 139
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • Butterfield DA, Drake J, Pocernich C, Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide. Trends Mol Med 2001; 7: 548-54.
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 140
    • 0035753031 scopus 로고    scopus 로고
    • Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases
    • Tabner BJ, Turnbull S, El-Agnaf O, Allsop D. Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases. Curr Top Med Chem 2001; 1: 507-17.
    • (2001) Curr Top Med Chem , vol.1 , pp. 507-517
    • Tabner, B.J.1    Turnbull, S.2    El-Agnaf, O.3    Allsop, D.4
  • 141
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery WR. Oxidative stress hypothesis in Alzheimer's disease. Free Radical Biol Med 1997; 23: 134-47.
    • (1997) Free Radical Biol Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 142
    • 0032890439 scopus 로고    scopus 로고
    • Alzheimer's disease and oxidative stress: Implications for novel therapeutic approaches
    • Behl C. Alzheimer's disease and oxidative stress: Implications for novel therapeutic approaches. Prog Neurobiol 1999; 57: 301-23.
    • (1999) Prog Neurobiol , vol.57 , pp. 301-323
    • Behl, C.1
  • 143
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994; 77: 817-27.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 144
    • 0141594627 scopus 로고    scopus 로고
    • Copper, beta-amyloid, and Alzheimer's disease: Tapping a sensitive connection
    • Bush AI, Masters CL, Tanzi RE. Copper, beta-amyloid, and Alzheimer's disease: Tapping a sensitive connection. Proc Natl Acad Sci USA 2003; 100: 11193-4.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11193-11194
    • Bush, A.I.1    Masters, C.L.2    Tanzi, R.E.3
  • 145
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith MA, Harris PL, Sayre LM, Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci USA 1997; 94: 9866-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 146
    • 2942729775 scopus 로고    scopus 로고
    • Metals in our minds: Therapeutic implications for neurodegenerative disorders
    • Doraiswamy PM, Finefrock AE. Metals in our minds: Therapeutic implications for neurodegenerative disorders. Lancet Neurol 2004; 3: 431-4.
    • (2004) Lancet Neurol , vol.3 , pp. 431-434
    • Doraiswamy, P.M.1    Finefrock, A.E.2
  • 147
    • 33745726690 scopus 로고    scopus 로고
    • Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis)
    • Gaggelli E, Kozlowski H, Valensin D, Valensin G. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem Rev 2006; 106: 1995-2044.
    • (2006) Chem Rev , vol.106 , pp. 1995-2044
    • Gaggelli, E.1    Kozlowski, H.2    Valensin, D.3    Valensin, G.4
  • 148
    • 33745173188 scopus 로고    scopus 로고
    • Anti-amyloidogenic effects of antioxidants: Implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K, Hamaguchi T, Naiki H, Yamada M. Anti-amyloidogenic effects of antioxidants: Implications for the prevention and therapeutics of Alzheimer's disease. Biochim Biophys Acta 2006; 1762: 575-86.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 575-586
    • Ono, K.1    Hamaguchi, T.2    Naiki, H.3    Yamada, M.4
  • 149
    • 0035235476 scopus 로고    scopus 로고
    • Neuroprotective abilities of resveratrol and other red wine constituents against nitric oxide-related toxicity in cultured hippocampal neurons
    • Bastianetto S, Zheng WH, Quirion R. Neuroprotective abilities of resveratrol and other red wine constituents against nitric oxide-related toxicity in cultured hippocampal neurons. Br J Pharmacol 2000; 131: 711-20.
    • (2000) Br J Pharmacol , vol.131 , pp. 711-720
    • Bastianetto, S.1    Zheng, W.H.2    Quirion, R.3
  • 150
    • 0035930961 scopus 로고    scopus 로고
    • The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons
    • Choi YT, Jung CH, Lee SR, Bae JH, Baek WK, Suh MH, et al. The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons. Life Sci 2001; 70: 603-14.
    • (2001) Life Sci , vol.70 , pp. 603-614
    • Choi, Y.T.1    Jung, C.H.2    Lee, S.R.3    Bae, J.H.4    Baek, W.K.5    Suh, M.H.6
  • 151
    • 0034851553 scopus 로고    scopus 로고
    • Levites Y, Weinreb O, Maor G, Youdim MB, Mandel S. Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration. J Neurochem 2001; 78: 1073-82.
    • Levites Y, Weinreb O, Maor G, Youdim MB, Mandel S. Green tea polyphenol (-)-epigallocatechin-3-gallate prevents N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration. J Neurochem 2001; 78: 1073-82.
  • 152
    • 0032432385 scopus 로고    scopus 로고
    • Oral administration of (-)catechin protects against ischemia-reperfusion-induced neuronal death in the gerbil
    • Inanami O, Watanabe Y, Syuto B, Nakano M, Tsuji M, Kuwabara M. Oral administration of (-)catechin protects against ischemia-reperfusion-induced neuronal death in the gerbil. Free Radical Res 1998; 29: 359-65.
    • (1998) Free Radical Res , vol.29 , pp. 359-365
    • Inanami, O.1    Watanabe, Y.2    Syuto, B.3    Nakano, M.4    Tsuji, M.5    Kuwabara, M.6
  • 153
    • 0032901807 scopus 로고    scopus 로고
    • Influence of the antioxidant quercetin in vivo on the level of nitric oxide determined by electron paramagnetic resonance in rat brain during global ischemia and reperfusion
    • Shutenko Z, Henry Y, Pinard E, Seylaz J, Potier P, Berthet F, et al. Influence of the antioxidant quercetin in vivo on the level of nitric oxide determined by electron paramagnetic resonance in rat brain during global ischemia and reperfusion. Biochem Pharmacol 1999; 57: 199-208.
    • (1999) Biochem Pharmacol , vol.57 , pp. 199-208
    • Shutenko, Z.1    Henry, Y.2    Pinard, E.3    Seylaz, J.4    Potier, P.5    Berthet, F.6
  • 154
    • 0033993607 scopus 로고    scopus 로고
    • Partial neuroprotection of in vivo excitotoxic brain damage by chronic administration of the red wine antioxidant agent, trans-resveratrol in rats
    • Virgili M, Contestabile A. Partial neuroprotection of in vivo excitotoxic brain damage by chronic administration of the red wine antioxidant agent, trans-resveratrol in rats. Neurosci Lett 2000; 281: 123-6.
    • (2000) Neurosci Lett , vol.281 , pp. 123-126
    • Virgili, M.1    Contestabile, A.2
  • 155
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's beta-amyloid fibril formation in vitro
    • Naiki H, Hasegawa K, Yamaguchi I, Nakamura H, Gejyo F, Nakakuki K. Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's beta-amyloid fibril formation in vitro. Biochemistry 1998; 37: 17882-9.
    • (1998) Biochemistry , vol.37 , pp. 17882-17889
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Gejyo, F.5    Nakakuki, K.6
  • 156
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's beta-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M. Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's beta-amyloid fibrils in vitro. Biochim Biophys Acta 2004; 1690: 193-202.
    • (2004) Biochim Biophys Acta , vol.1690 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 157
    • 0036313066 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's beta-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Yoshiike Y, Takashima A, Yamada M, Naiki H. Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's beta-amyloid fibrils in vitro. J Neurochem 2002; 81: 434-40.
    • (2002) J Neurochem , vol.81 , pp. 434-440
    • Ono, K.1    Hasegawa, K.2    Yoshiike, Y.3    Takashima, A.4    Yamada, M.5    Naiki, H.6
  • 158
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M. Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease. J Neurochem 2003; 87: 172-81.
    • (2003) J Neurochem , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 159
    • 0031727043 scopus 로고    scopus 로고
    • Study on the inhibitory effect of tannins and flavonoids against the 1,1-diphenyl-2 picrylhydrazyl radical
    • Yokozawa T, Chen CP, Dong E, Tanaka T, Nonaka GI, Nishioka I. Study on the inhibitory effect of tannins and flavonoids against the 1,1-diphenyl-2 picrylhydrazyl radical. Biochem Pharmacol 1998; 56: 213-22.
    • (1998) Biochem Pharmacol , vol.56 , pp. 213-222
    • Yokozawa, T.1    Chen, C.P.2    Dong, E.3    Tanaka, T.4    Nonaka, G.I.5    Nishioka, I.6
  • 160
    • 0020966949 scopus 로고
    • Studies on the activities of tannins and related compounds from medicinal plants and drugs. I. Inhibitory effects on lipid peroxidation in mitochondria and microsomes of liver
    • Okuda T, Kimura Y, Yoshida T, Hatano T, Okuda H, Arichi S. Studies on the activities of tannins and related compounds from medicinal plants and drugs. I. Inhibitory effects on lipid peroxidation in mitochondria and microsomes of liver. Chem Pharm Bull 1983; 31: 1625-31.
    • (1983) Chem Pharm Bull , vol.31 , pp. 1625-1631
    • Okuda, T.1    Kimura, Y.2    Yoshida, T.3    Hatano, T.4    Okuda, H.5    Arichi, S.6
  • 161
    • 0024784639 scopus 로고
    • Antioxidant functions of carotenoids
    • Krinsky NI. Antioxidant functions of carotenoids. Free Radical Biol Med 1989; 7: 617-35.
    • (1989) Free Radical Biol Med , vol.7 , pp. 617-635
    • Krinsky, N.I.1
  • 163
    • 0032563234 scopus 로고    scopus 로고
    • Ascorbic acid prevents beta-amyloid-induced intracellular calcium increase and cell death in PC12 cells
    • Yallampalli S, Micci MA, Taglialatela G. Ascorbic acid prevents beta-amyloid-induced intracellular calcium increase and cell death in PC12 cells. Neurosci Lett 1998; 251: 105-8.
    • (1998) Neurosci Lett , vol.251 , pp. 105-108
    • Yallampalli, S.1    Micci, M.A.2    Taglialatela, G.3
  • 164
  • 165
    • 4544227975 scopus 로고    scopus 로고
    • Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M. Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro. Exp Neurol 2004; 189: 380-92.
    • (2004) Exp Neurol , vol.189 , pp. 380-392
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 166
    • 0032497593 scopus 로고    scopus 로고
    • Universal template approach to drug design: Polyamines as selective muscarinic receptor antagonists
    • Bolognesi ML, Minarini A, Budriesi R, Cacciaguerra S, Chiarini A, Spampinato S, et al. Universal template approach to drug design: polyamines as selective muscarinic receptor antagonists. J Med Chem 1998; 41: 4150-60.
    • (1998) J Med Chem , vol.41 , pp. 4150-4160
    • Bolognesi, M.L.1    Minarini, A.2    Budriesi, R.3    Cacciaguerra, S.4    Chiarini, A.5    Spampinato, S.6
  • 168
    • 34948904272 scopus 로고    scopus 로고
    • Novel class of quinone-bearing polyamines as multitarget-directed ligands to combat Alzheimer's disease
    • Bolognesi ML, Banzi R, Bartolini M, Cavalli A, Tarozzi A, Andrisano V, et al. Novel class of quinone-bearing polyamines as multitarget-directed ligands to combat Alzheimer's disease. J Med Chem 2007; 50: 4882-97.
    • (2007) J Med Chem , vol.50 , pp. 4882-4897
    • Bolognesi, M.L.1    Banzi, R.2    Bartolini, M.3    Cavalli, A.4    Tarozzi, A.5    Andrisano, V.6
  • 169
    • 0028116941 scopus 로고
    • Total antioxidant status in plasma and body fluids
    • Rice-Evans C, Miller NJ. Total antioxidant status in plasma and body fluids. Methods Enzymol 1994; 234: 279-93.
    • (1994) Methods Enzymol , vol.234 , pp. 279-293
    • Rice-Evans, C.1    Miller, N.J.2
  • 170
    • 0031885039 scopus 로고    scopus 로고
    • Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone)
    • Mordente A, Martorana GE, Minotti G, Giardina B. Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone). Chem Res Toxicol 1998; 11: 54-63.
    • (1998) Chem Res Toxicol , vol.11 , pp. 54-63
    • Mordente, A.1    Martorana, G.E.2    Minotti, G.3    Giardina, B.4
  • 171
    • 39049192182 scopus 로고    scopus 로고
    • On the molecular basis linking Nerve Growth Factor (NGF) to Alzheimer's disease
    • Capsoni S, Cattaneo A. On the molecular basis linking Nerve Growth Factor (NGF) to Alzheimer's disease. Cell Mol Neurobiol 2006; 26: 619-33.
    • (2006) Cell Mol Neurobiol , vol.26 , pp. 619-633
    • Capsoni, S.1    Cattaneo, A.2
  • 173
    • 0033951505 scopus 로고    scopus 로고
    • Alzheimer's disease and inflammation: A review of cellular and therapeutic mechanisms
    • Halliday G, Robinson SR, Shepherd C, Kril J. Alzheimer's disease and inflammation: A review of cellular and therapeutic mechanisms. Clin Exp Pharmacol Physiol 2000; 27: 1-8.
    • (2000) Clin Exp Pharmacol Physiol , vol.27 , pp. 1-8
    • Halliday, G.1    Robinson, S.R.2    Shepherd, C.3    Kril, J.4
  • 174
    • 0032944604 scopus 로고    scopus 로고
    • Inflammation of the brain in Alzheimer's disease: Implications for therapy
    • McGeer PL, McGeer EG. Inflammation of the brain in Alzheimer's disease:
    • (1999) J Leukoc Biol , vol.65 , pp. 409-415
    • McGeer, P.L.1    McGeer, E.G.2
  • 175
    • 0036162905 scopus 로고    scopus 로고
    • New drugs for Alzheimer's disease and other dementias
    • Bullock R. New drugs for Alzheimer's disease and other dementias. Br J Psychiatry 2002; 180: 135-9.
    • (2002) Br J Psychiatry , vol.180 , pp. 135-139
    • Bullock, R.1
  • 176
    • 2542509435 scopus 로고    scopus 로고
    • Anti-inflammatory substances - a new therapeutic option in Alzheimer's disease
    • Hull M, Fiebich BL, Schumann G, Lieb K, Bauer J. Anti-inflammatory substances - a new therapeutic option in Alzheimer's disease. Drug Discov Today 1999; 4: 275-82.
    • (1999) Drug Discov Today , vol.4 , pp. 275-282
    • Hull, M.1    Fiebich, B.L.2    Schumann, G.3    Lieb, K.4    Bauer, J.5
  • 177
    • 0034924557 scopus 로고    scopus 로고
    • Cyclooxygenase and Alzheimer's disease: Implications for preventive initiatives to slow the progression of clinical dementia
    • Pasinetti GM. Cyclooxygenase and Alzheimer's disease: Implications for preventive initiatives to slow the progression of clinical dementia. Arch Gerontol Geriatr 2001; 33: 13-28.
    • (2001) Arch Gerontol Geriatr , vol.33 , pp. 13-28
    • Pasinetti, G.M.1
  • 178
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer PL, Schulzer M, McGeer EG. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies. Neurology 1996; 47: 425-32.
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 179
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • Stewart WF, Kawas C, Corrada M, Metter EJ. Risk of Alzheimer's disease and duration of NSAID use. Neurology 1997; 48: 626-32.
    • (1997) Neurology , vol.48 , pp. 626-632
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 180
    • 0034254924 scopus 로고    scopus 로고
    • Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer's disease
    • Lim GP, Yang F, Chu T, Chen P, Beech W, Teter B, et al. Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer's disease. J Neurosci 2000; 20: 5709-14.
    • (2000) J Neurosci , vol.20 , pp. 5709-5714
    • Lim, G.P.1    Yang, F.2    Chu, T.3    Chen, P.4    Beech, W.5    Teter, B.6
  • 181
    • 0037638809 scopus 로고    scopus 로고
    • Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: A randomized controlled trial
    • Aisen PS, Schafer KA, Grundman M, Pfeiffer E, Sano M, Davis KL, et al. Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: A randomized controlled trial. JAMA 2003; 289: 2819-26.
    • (2003) JAMA , vol.289 , pp. 2819-2826
    • Aisen, P.S.1    Schafer, K.A.2    Grundman, M.3    Pfeiffer, E.4    Sano, M.5    Davis, K.L.6
  • 182
    • 27744462871 scopus 로고    scopus 로고
    • Deletion of the prostaglandin E2 EP2 receptor reduces oxidative damage and amyloid burden in a model of Alzheimer's disease
    • Liang X, Wang Q, Hand T, Wu L, Breyer RM, Montine TJ, et al. Deletion of the prostaglandin E2 EP2 receptor reduces oxidative damage and amyloid burden in a model of Alzheimer's disease. J Neurosci 2005; 25: 10180-7.
    • (2005) J Neurosci , vol.25 , pp. 10180-10187
    • Liang, X.1    Wang, Q.2    Hand, T.3    Wu, L.4    Breyer, R.M.5    Montine, T.J.6
  • 183
    • 0034620538 scopus 로고    scopus 로고
    • A randomized controlled trial of prednisone in Alzheimer's disease. Alzheimer's Disease Cooperative Study
    • Aisen PS, Davis KL, Berg JD, Schafer K, Campbell K, Thomas RG, et al. A randomized controlled trial of prednisone in Alzheimer's disease. Alzheimer's Disease Cooperative Study. Neurology 2000; 54: 588-93.
    • (2000) Neurology , vol.54 , pp. 588-593
    • Aisen, P.S.1    Davis, K.L.2    Berg, J.D.3    Schafer, K.4    Campbell, K.5    Thomas, R.G.6
  • 184
    • 0033551547 scopus 로고    scopus 로고
    • A double-blind, placebo-controlled trial of diclofenac/misoprostol in Alzheimer's disease
    • Scharf S, Mander A, Ugoni A, Vajda F, Christophidis N. A double-blind, placebo-controlled trial of diclofenac/misoprostol in Alzheimer's disease. Neurology 1999; 53: 197-201.
    • (1999) Neurology , vol.53 , pp. 197-201
    • Scharf, S.1    Mander, A.2    Ugoni, A.3    Vajda, F.4    Christophidis, N.5
  • 185
    • 0035968743 scopus 로고    scopus 로고
    • Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-beta aggregation
    • Thomas T, Nadackal TG, Thomas K. Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-beta aggregation. Neuroreport 2001; 12: 3263-7.
    • (2001) Neuroreport , vol.12 , pp. 3263-3267
    • Thomas, T.1    Nadackal, T.G.2    Thomas, K.3
  • 186
    • 0037475148 scopus 로고    scopus 로고
    • In vitro detection of (S)-naproxen and ibuprofen binding to plaques in the Alzheimer's brain using the positron emission tomography molecular imaging probe 2-(1-[6-[(2-[(18)]Ffluoroethyl) (methyl)amino-2-naphthylethylidene)malono nitrile
    • Agdeppa ED, Kepe V, Petri A, Satyamurthy N, Liu J, Huang SC, et al. In vitro detection of (S)-naproxen and ibuprofen binding to plaques in the Alzheimer's brain using the positron emission tomography molecular imaging probe 2-(1-[6-[(2-[(18)]Ffluoroethyl) (methyl)amino-2-naphthylethylidene)malono nitrile. Neuroscience 2003; 117: 723-30.
    • (2003) Neuroscience , vol.117 , pp. 723-730
    • Agdeppa, E.D.1    Kepe, V.2    Petri, A.3    Satyamurthy, N.4    Liu, J.5    Huang, S.C.6
  • 187
    • 0035893245 scopus 로고    scopus 로고
    • Binding characteristics of radiofluorinated 6-dialkylamino-2-naphthylethylidene derivatives as positron emission tomography imaging probes for beta-amyloid plaques in Alzheimer's disease
    • Agdeppa ED, Kepe V, Liu J, Flores-Torres S, Satyamurthy N, Petric A, et al. Binding characteristics of radiofluorinated 6-dialkylamino-2-naphthylethylidene derivatives as positron emission tomography imaging probes for beta-amyloid plaques in Alzheimer's disease. J Neurosci 2001; 21: RC189.
    • (2001) J Neurosci , vol.21
    • Agdeppa, E.D.1    Kepe, V.2    Liu, J.3    Flores-Torres, S.4    Satyamurthy, N.5    Petric, A.6
  • 188
    • 65649142359 scopus 로고    scopus 로고
    • Pipeline and commercial insight: Alzheimer's disease - beta treatments on the horizon
    • 2005. Report No, DMHC2121
    • Lynch L. Pipeline and commercial insight: Alzheimer's disease - beta treatments on the horizon. Research report: Datamonitor; 2005. Report No.: DMHC2121.
    • Research report: Datamonitor
    • Lynch, L.1
  • 189
    • 48949117577 scopus 로고    scopus 로고
    • The role of the cell surface LRP and soluble LRP in blood-brain barrier Abeta clearance in Alzheimer's disease
    • Deane R, Sagare A, Zlokovic BV. The role of the cell surface LRP and soluble LRP in blood-brain barrier Abeta clearance in Alzheimer's disease. Curr Pharm Des 2008; 14(16): 1601-5.
    • (2008) Curr Pharm Des , vol.14 , Issue.16 , pp. 1601-1605
    • Deane, R.1    Sagare, A.2    Zlokovic, B.V.3
  • 191
    • 43049158125 scopus 로고    scopus 로고
    • Designing transient binding drugs: A new concept for drug discovery
    • Ohlson S. Designing transient binding drugs: A new concept for drug discovery. Drug Discov Today 2008; 13(9-10): 433-9.
    • (2008) Drug Discov Today , vol.13 , Issue.9-10 , pp. 433-439
    • Ohlson, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.