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Volumn 175, Issue 6, 2009, Pages 2557-2565

Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-β aggregation pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CURCUMIN; FERULIC ACID; MONOMER; MYRICETIN; NORDIHYDROGUAIARETIC ACID; OLIGOMER; ROSMARINIC ACID; TROMETAMOL;

EID: 73549106551     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.2353/ajpath.2009.090417     Document Type: Article
Times cited : (374)

References (75)
  • 2
    • 0028945660 scopus 로고
    • Evidence that Aβ42 is the real culprit in Alzheimer's disease
    • Younkin SG: Evidence that Aβ42 is the real culprit in Alzheimer's disease. Ann Neurol 1995, 37:287-288
    • (1995) Ann Neurol , vol.37 , pp. 287-288
    • Younkin, S.G.1
  • 3
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe DJ: Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 1999, 399:A23-31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 5
    • 0345669752 scopus 로고    scopus 로고
    • Alzheimer's disease: The cholesterol connection
    • Puglielli L, Tanzi RE, Kovacs DM: Alzheimer's disease: the cholesterol connection. Nat Neurosci 2003, 6:345-351
    • (2003) Nat Neurosci , vol.6 , pp. 345-351
    • Puglielli, L.1    Tanzi, R.E.2    Kovacs, D.M.3
  • 6
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW: Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984, 120:885-890
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 7
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW: Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984, 122:1131-1135
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 9
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D, Lerman MI, McBride OW, Saffiotti U, Gajdusek DC: Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 1987, 235:877-880
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 11
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • Robakis NK, Ramakrishna N, Wolfe G, Wisniewski HM: Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides. Proc Natl Acad Sci USA: 1987, 84:4190-4194
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 13
    • 0014481635 scopus 로고
    • Presenile dementia and Alzheimer's disease in mongolism
    • Olson MI, Shaw CM: Presenile dementia and Alzheimer's disease in mongolism. Brain 1969, 92:147-156
    • (1969) Brain , vol.92 , pp. 147-156
    • Olson, M.I.1    Shaw, C.M.2
  • 15
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid
    • Mullan M, Crawford F, Axelman K, Houlden H, Lilius L, Winblad B, Lannfelt L: A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid. Nat Genet 1992, 1:345-347
    • (1992) Nat Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3    Houlden, H.4    Lilius, L.5    Winblad, B.6    Lannfelt, L.7
  • 18
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ: Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 1999, 398:513-517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 19
    • 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, 1762:575-586
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 575-586
    • Ono, K.1    Hamaguchi, T.2    Naiki, H.3    Yamada, M.4
  • 20
    • 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, 63:1538-1552
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1538-1552
    • Hamaguchi, T.1    Ono, K.2    Yamada, M.3
  • 21
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - a decade of discovery
    • Walsh DM, Selkoe DJ: Aβ oligomers - a decade of discovery. J Neurochem 2007, 101:1172-1184
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 22
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid-β-peptide
    • Haass C, Selkoe DJ: Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid-β-peptide. Nat Rev Mol Cell Biol 2007, 8:101-112
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 23
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid-β-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein WL, Stine WB Jr, Teplow DB: Small assemblies of unmodified amyloid-β-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 2004, 25:569-580
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr, W.B.2    Teplow, D.B.3
  • 24
    • 0035993237 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimer's disease: Globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein WL: Aβ toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Int 2002, 41:345-352
    • (2002) Neurochem Int , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 25
    • 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, 297:353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 26
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid-β oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, Glabe CG: Small molecule inhibitors of aggregation indicate that amyloid-β oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 2007, 282: 10311-10324
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 27
    • 15444372049 scopus 로고    scopus 로고
    • Preformed β-amyloid fibrils are destabilized by coenzyme Q10 in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M: Preformed β-amyloid fibrils are destabilized by coenzyme Q10 in vitro. Biochem Biophys Res Commun 2005, 330:111-116
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 111-116
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 28
    • 24644438783 scopus 로고    scopus 로고
    • Ferulic acid destabilizes preformed β-amyloid fibrils in vitro
    • Ono K, Hirohata M, Yamada M: Ferulic acid destabilizes preformed β-amyloid fibrils in vitro. Biochem Biophys Res Commun 2005, 336: 444-449
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 444-449
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 29
    • 32344435392 scopus 로고    scopus 로고
    • Alpha-lipoic acid exhibits anti-amyloidogenicity for β-amyloid fibrils in vitro
    • Ono K, Hirohata M, Yamada M: Alpha-lipoic acid exhibits anti-amyloidogenicity for β-amyloid fibrils in vitro. Biochem Biophys Res Commun 2006, 341:1046-1052
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 1046-1052
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 30
    • 33847025338 scopus 로고    scopus 로고
    • The anti-amyloidogenic effect is exerted against Alzheimer's β-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure
    • Hirohata M, Hasegawa K, Tsutsumi-Yasuhara S, Ohhashi Y, Ookoshi T, Ono K, Yamada M, Naiki H: The anti-amyloidogenic effect is exerted against Alzheimer's β-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure. Biochemistry 2007, 46:1888-1899
    • (2007) Biochemistry , vol.46 , pp. 1888-1899
    • Hirohata, M.1    Hasegawa, K.2    Tsutsumi-Yasuhara, S.3    Ohhashi, Y.4    Ookoshi, T.5    Ono, K.6    Yamada, M.7    Naiki, H.8
  • 31
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-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 β-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
  • 32
    • 0036838889 scopus 로고    scopus 로고
    • Nicotine breaks down preformed Alzheimer's β-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Yamada M, Naiki H: Nicotine breaks down preformed Alzheimer's β-amyloid fibrils in vitro. Biol Psychiatry 2002, 52:880-886
    • (2002) Biol Psychiatry , vol.52 , pp. 880-886
    • Ono, K.1    Hasegawa, K.2    Yamada, M.3    Naiki, H.4
  • 33
    • 0036313066 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's β-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 β-amyloid fibrils in vitro. J Neurochem 2002, 81:434-440
    • (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
  • 34
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M: Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J Neurosci Res 2004, 75:742-750
    • (2004) J Neurosci Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 35
    • 31744447521 scopus 로고    scopus 로고
    • Anti-Parkinsonian agents have anti-amyloidogenic activity for Alzheimer's β-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M: Anti-Parkinsonian agents have anti-amyloidogenic activity for Alzheimer's β-amyloid fibrils in vitro. Neurochem Int 2006, 48:275-285
    • (2006) Neurochem Int , vol.48 , pp. 275-285
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 36
    • 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, 87:172-181
    • (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
  • 37
    • 57749112087 scopus 로고    scopus 로고
    • Effects of grape seed-derived polyphenols on amyloid-β-protein self-assembly and cytotoxicity
    • Ono K, Condron MM, Ho L, Wang J, Zhao W, Pasinetti GM, Teplow DB: Effects of grape seed-derived polyphenols on amyloid-β-protein self-assembly and cytotoxicity. J Biol Chem 2008, 283:32176-32187
    • (2008) J Biol Chem , vol.283 , pp. 32176-32187
    • Ono, K.1    Condron, M.M.2    Ho, L.3    Wang, J.4    Zhao, W.5    Pasinetti, G.M.6    Teplow, D.B.7
  • 38
    • 46749123053 scopus 로고    scopus 로고
    • Grape-derived polyphenolics prevent Aβ oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer's disease
    • Wang J, Ho L, Zhao W, Ono K, Rosensweig C, Chen L, Humala N, Teplow DB, Pasinetti GM: Grape-derived polyphenolics prevent Aβ oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer's disease. J Neurosci 2008, 28:6388-6392
    • (2008) J Neurosci , vol.28 , pp. 6388-6392
    • Wang, J.1    Ho, L.2    Zhao, W.3    Ono, K.4    Rosensweig, C.5    Chen, L.6    Humala, N.7    Teplow, D.B.8    Pasinetti, G.M.9
  • 40
    • 34547451145 scopus 로고    scopus 로고
    • Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model
    • Garcia-Alloza M, Borrelli LA, Rozkalne A, Hyman BT, Bacskai BJ: Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model. J Neurochem 2007, 102:1095-1104
    • (2007) J Neurochem , vol.102 , pp. 1095-1104
    • Garcia-Alloza, M.1    Borrelli, L.A.2    Rozkalne, A.3    Hyman, B.T.4    Bacskai, B.J.5
  • 41
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, Beech W, Frautschy SA, Cole GM: The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 2001, 21:8370-8377
    • (2001) J Neurosci , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 44
  • 47
    • 32544435900 scopus 로고    scopus 로고
    • Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: A follow-up study
    • Hansson O, Zetterberg H, Buchhave P, Londos E, Blennow K, Minthon L: Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: a follow-up study. Lancet Neurol 2006, 5:228-234
    • (2006) Lancet Neurol , vol.5 , pp. 228-234
    • Hansson, O.1    Zetterberg, H.2    Buchhave, P.3    Londos, E.4    Blennow, K.5    Minthon, L.6
  • 52
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG: Structural classification of toxic amyloid oligomers. J Biol Chem 2008, 283:29639-29643
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 55
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA: β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA: 1994, 91:12243-12247
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 57
    • 34248210710 scopus 로고    scopus 로고
    • A natural scavenger of peroxynitrites, rosmarinic acid, protects against impairment of memory induced by Aβ(25-35)
    • Alkam T, Nitta A, Mizoguchi H, Itoh A, Nabeshima T: A natural scavenger of peroxynitrites, rosmarinic acid, protects against impairment of memory induced by Aβ(25-35). Behav Brain Res 2007, 180:139-145
    • (2007) Behav Brain Res , vol.180 , pp. 139-145
    • Alkam, T.1    Nitta, A.2    Mizoguchi, H.3    Itoh, A.4    Nabeshima, T.5
  • 58
    • 33646772566 scopus 로고    scopus 로고
    • The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-β peptide-induced neurotoxicity
    • Iuvone T, De Filippis D, Esposito G, D'Amico A, Izzo AA: The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-β peptide-induced neurotoxicity. J Pharmacol Exp Ther 2006, 317:1143-1149
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 1143-1149
    • Iuvone, T.1    De Filippis, D.2    Esposito, G.3    D'Amico, A.4    Izzo, A.A.5
  • 61
    • 0027959041 scopus 로고
    • Nordihydroguaiaretic acid protects hippocampal neurons against amyloid-β-peptide toxicity, and attenuates free radical and calcium accumulation
    • Goodman Y, Steiner MR, Steiner SM, Mattson MP: Nordihydroguaiaretic acid protects hippocampal neurons against amyloid-β-peptide toxicity, and attenuates free radical and calcium accumulation. Brain Res 1994, 654:171-176
    • (1994) Brain Res , vol.654 , pp. 171-176
    • Goodman, Y.1    Steiner, M.R.2    Steiner, S.M.3    Mattson, M.P.4
  • 62
    • 0024652076 scopus 로고
    • Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals
    • Zhao BL, Li XJ, He RG, Cheng SJ, Xin WJ: Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals. Cell Biophys 1989, 14:175-185
    • (1989) Cell Biophys , vol.14 , pp. 175-185
    • Zhao, B.L.1    Li, X.J.2    He, R.G.3    Cheng, S.J.4    Xin, W.J.5
  • 63
    • 0031033145 scopus 로고    scopus 로고
    • Nitric oxide scavenging by curcuminoids
    • Sreejayan, Rao MN: Nitric oxide scavenging by curcuminoids. J Pharm Pharmacol 1997, 49:105-107
    • (1997) J Pharm Pharmacol , vol.49 , pp. 105-107
    • Sreejayan, R.M.N.1
  • 64
    • 0035957872 scopus 로고    scopus 로고
    • Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult
    • Kim DS, Park SY, Kim JK: Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult. Neurosci Lett 2001, 303:57-61
    • (2001) Neurosci Lett , vol.303 , pp. 57-61
    • Kim, D.S.1    Park, S.Y.2    Kim, J.K.3
  • 66
    • 0033826684 scopus 로고    scopus 로고
    • The health benefits of wine
    • German JB, Walzem RL: The health benefits of wine. Annu Rev Nutr 2000, 20:561-593
    • (2000) Annu Rev Nutr , vol.20 , pp. 561-593
    • German, J.B.1    Walzem, R.L.2
  • 68
    • 0037063448 scopus 로고    scopus 로고
    • Flavonoids and antioxidant capacity of Georgiagrown Vidalia onions
    • Sellappan S, Akoh CC: Flavonoids and antioxidant capacity of Georgiagrown Vidalia onions. J Agric Food Chem 2002, 50:5338-5342
    • (2002) J Agric Food Chem , vol.50 , pp. 5338-5342
    • Sellappan, S.1    Akoh, C.C.2
  • 69
    • 0030747399 scopus 로고    scopus 로고
    • Biological effects of myricetin
    • Ong KC, Khoo HE: Biological effects of myricetin. Gen Pharmacol 1997, 29:121-126
    • (1997) Gen Pharmacol , vol.29 , pp. 121-126
    • Ong, K.C.1    Khoo, H.E.2
  • 70
    • 45049086920 scopus 로고    scopus 로고
    • Flavonols and flavones as BACE-1 inhibitors: Structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features
    • Shimmyo Y, Kihara T, Akaike A, Niidome T, Sugimoto H: Flavonols and flavones as BACE-1 inhibitors: structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features. Biochim Biophys Acta 2008, 1780:819-825
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 819-825
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 71
    • 0026688245 scopus 로고
    • Antioxidant potential of ferulic acid
    • Graf E: Antioxidant potential of ferulic acid. Free Radic Biol Med 1992, 13:435-448
    • (1992) Free Radic Biol Med , vol.13 , pp. 435-448
    • Graf, E.1
  • 73
    • 3442891510 scopus 로고    scopus 로고
    • Inhibitory effects of long-term administration of ferulic acid on microglial activation induced by intracerebroventricular injection of β-amyloid peptide (1-42) in mice
    • Kim HS, Cho JY, Kim DH, Yan JJ, Lee HK, Suh HW, Song DK: Inhibitory effects of long-term administration of ferulic acid on microglial activation induced by intracerebroventricular injection of β-amyloid peptide (1-42) in mice. Biol Pharm Bull 2004, 27:120-121
    • (2004) Biol Pharm Bull , vol.27 , pp. 120-121
    • Kim, H.S.1    Cho, J.Y.2    Kim, D.H.3    Yan, J.J.4    Lee, H.K.5    Suh, H.W.6    Song, D.K.7
  • 75
    • 13644265462 scopus 로고    scopus 로고
    • Ferulic acid ethyl ester protects neurons against amyloid-β-peptide(1-42)- induced oxidative stress and neurotoxicity: Relationship to antioxidant activity
    • Sultana R, Ravagna A, Mohmmad-Abdul H, Calabrese V, Butterfield DA: Ferulic acid ethyl ester protects neurons against amyloid-β-peptide(1-42)- induced oxidative stress and neurotoxicity: relationship to antioxidant activity. J Neurochem 2005, 92:749-758
    • (2005) J Neurochem , vol.92 , pp. 749-758
    • Sultana, R.1    Ravagna, A.2    Mohmmad-Abdul, H.3    Calabrese, V.4    Butterfield, D.A.5


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