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Volumn 287, Issue 18, 2012, Pages 14631-14643

Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROCESS; ALZHEIMER DISEASE; ASSEMBLY PROCESS; CELLULAR TOXICITIES; IN-VITRO; INVARIANT FEATURES; MYRICETIN; PHENOLIC COMPOUNDS; ROSMARINIC ACID; SHIFT CHANGES; SITE-SPECIFIC;

EID: 84860386735     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.325456     Document Type: Article
Times cited : (210)

References (54)
  • 1
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass, C., and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer amyloid β peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 2
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid β protein assembly and Alzheimer disease
    • Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid β protein assembly and Alzheimer disease. J. Biol. Chem. 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 3
    • 79952563494 scopus 로고    scopus 로고
    • Low-n oligomers as therapeutic targets of Alzheimer disease
    • Ono, K., and Yamada, M. (2011) Low-n oligomers as therapeutic targets of Alzheimer disease. J. Neurochem. 117, 19-28
    • (2011) J. Neurochem. , vol.117 , pp. 19-28
    • Ono, K.1    Yamada, M.2
  • 4
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., and Selkoe, D. J. (2006) Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers. J. Physiol. 572, 477-492
    • (2006) J. Physiol. , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 5
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., and Sabatini, B. L. (2007) Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27, 2866-2875 (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 7
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid β protein oligomers
    • Ono, K., Condron, M. M., and Teplow, D. B. (2009) Structure-neurotoxicity relationships of amyloid β protein oligomers. Proc. Natl. Acad. Sci. U.S.A. 106, 14745-14750
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 9
    • 0037069290 scopus 로고    scopus 로고
    • Amount and type of alcohol and risk of dementia: The Copenhagen City Heart Study
    • Truelsen, T., Thudium, D., Grønbaek, M., and Copenhagen City Heart Study (2002) Amount and type of alcohol and risk of dementia: The Copenhagen City Heart Study. Neurology 59, 1313-1319 (Pubitemid 35285979)
    • (2002) Neurology , vol.59 , Issue.9 , pp. 1313-1319
    • Truelsen, T.1    Thudium, D.2    Gronbaek, M.3
  • 10
  • 11
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer's disease amyloid-β peptides
    • DOI 10.1074/jbc.M508246200
    • Marambaud, P., Zhao, H., and Davies, P. (2005) Resveratrol promotes clearance of Alzheimer disease amyloid-β peptides. J. Biol. Chem. 280, 37377-37382 (Pubitemid 41642343)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 14
    • 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
    • DOI 10.1046/j.1471-4159.2003.01976.x
    • Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., and Yamada, M. (2003) Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer disease. J. Neurochem. 87, 172-181 (Pubitemid 37210651)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.1 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 15
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin Has Potent Anti-Amyloidogenic Effects for Alzheimer's β-Amyloid Fibrils In Vitro
    • DOI 10.1002/jnr.20025
    • Ono, K., Hasegawa, K., Naiki, H., and Yamada, M. (2004) Curcumin has potent anti-amyloidogenic effects for Alzheimer β-amyloid fibrils in vitro. J. Neurosci. Res. 75, 742-750 (Pubitemid 38296087)
    • (2004) Journal of Neuroscience Research , vol.75 , Issue.6 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 16
    • 24644438783 scopus 로고    scopus 로고
    • Ferulic acid destabilizes preformed β-amyloid fibrils in vitro
    • DOI 10.1016/j.bbrc.2005.08.148, PII S0006291X05017821
    • Ono, K., Hirohata, M., and Yamada, M. (2005) Ferulic acid destabilizes preformed β-amyloid fibrils in vitro. Biochem. Biophys. Res. Commun. 336, 444-449 (Pubitemid 41267250)
    • (2005) Biochemical and Biophysical Research Communications , vol.336 , Issue.2 , pp. 444-449
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 17
    • 46749123053 scopus 로고    scopus 로고
    • Grape-derived polyphenolics prevent Aβ oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer disease
    • Wang, J., Ho, L., Zhao, W., Ono, K., Rosensweig, C., Chen, L., Humala, N., Teplow, D. B., and Pasinetti, G. M. (2008) Grape-derived polyphenolics prevent Aβ oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer disease. J. Neurosci. 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
  • 18
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent Alzheimer pathology through different effects on the amyloid-β aggregation pathway
    • Hamaguchi, T., Ono, K., Murase, A., and Yamada, M. (2009) Phenolic compounds prevent Alzheimer pathology through different effects on the amyloid-β aggregation pathway. Am. J. Pathol. 175, 2557-2565
    • (2009) Am. J. Pathol. , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 19
    • 84870849843 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 20
    • 57749112087 scopus 로고    scopus 로고
    • Effects of grape seed-derived polyphenols on amyloid β protein self-assembly and cytotoxicity
    • Ono, K., Condron, M. M., Ho, L., Wang, J., Zhao, W., Pasinetti, G. M., and Teplow, D. B. (2008) Effects of grape seed-derived polyphenols on amyloid β protein self-assembly and cytotoxicity. J. Biol. Chem. 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
  • 22
    • 2942672221 scopus 로고    scopus 로고
    • Rapid photochemical cross-linking-a new tool for studies of metastable, amyloidogenic protein assemblies
    • Bitan, G., and Teplow, D. B. (2004) Rapid photochemical cross-linking-a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 37, 357-364
    • (2004) Acc. Chem. Res. , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 23
    • 77954927651 scopus 로고    scopus 로고
    • Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β protein assembly and toxicity
    • Ono, K., Condron, M. M., and Teplow, D. B. (2010) Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β protein assembly and toxicity. J. Biol. Chem. 285, 23186-23197
    • (2010) J. Biol. Chem. , vol.285 , pp. 23186-23197
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 24
    • 13444310701 scopus 로고    scopus 로고
    • Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution-state NMR upon variation of salt conditions
    • DOI 10.1021/bi048264b
    • Narayanan, S., and Reif, B. (2005) Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution-state NMR upon variation of salt conditions. Biochemistry 44, 1444-1452 (Pubitemid 40204388)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1444-1452
    • Narayanan, S.1    Reif, B.2
  • 25
    • 34247204257 scopus 로고    scopus 로고
    • Understanding the molecular basis for the inhibition of the Alzheimer's Aβ-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy
    • DOI 10.1021/ja067367+
    • Milojevic, J., Esposito, V., Das, R., and Melacini, G. (2007) Understanding the molecular basis for the inhibition of the Alzheimer Aβ-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy. J. Am. Chem. Soc. 129, 4282-4290 (Pubitemid 46603572)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.14 , pp. 4282-4290
    • Milojevic, J.1    Esposito, V.2    Das, R.3    Melacini, G.4
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 27
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study
    • DOI 10.1016/j.jmb.2007.02.093, PII S0022283607003105
    • Sgourakis, N. G., Yan, Y., McCallum, S. A., Wang, C., and Garcia, A. E. (2007) The Alzheimer peptides Aβ40 and 42 adopt distinct conformations in water: A combined MD/NMR study. J. Mol. Biol. 368, 1448-1457 (Pubitemid 46617600)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.2    McCallum, S.A.3    Wang, C.4    Garcia, A.E.5
  • 28
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 31
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • DOI 10.1073/pnas.96.11.6020
    • Fancy, D. A., and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light. Proc. Natl. Acad. Sci. U.S.A. 96, 6020-6024 (Pubitemid 29256612)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 32
    • 33751106208 scopus 로고    scopus 로고
    • Aβ42 is More Rigid than Aβ40 at the C Terminus: Implications for Aβ Aggregation and Toxicity
    • DOI 10.1016/j.jmb.2006.09.046, PII S0022283606012551
    • Yan, Y., and Wang, C. (2006) Aβ42 is more rigid than Aβ40 at the C terminus: Implications for Aβ aggregation and toxicity. J. Mol. Biol. 364, 853-862 (Pubitemid 44765041)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.5 , pp. 853-862
    • Yan, Y.1    Wang, C.2
  • 33
    • 72249108028 scopus 로고    scopus 로고
    • Human serum albumin inhibits Aβ fibrillization through a "monomer-competitor" mechanism
    • Milojevic, J., Raditsis, A., and Melacini, G. (2009) Human serum albumin inhibits Aβ fibrillization through a "monomer-competitor" mechanism. Biophys. J. 97, 2585-2594
    • (2009) Biophys. J. , vol.97 , pp. 2585-2594
    • Milojevic, J.1    Raditsis, A.2    Melacini, G.3
  • 34
    • 43949103402 scopus 로고    scopus 로고
    • Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides
    • DOI 10.1021/jp7118718
    • Huang, H., Milojevic, J., and Melacini, G. (2008) Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides. J. Phys. Chem. B 112, 5795-5802 (Pubitemid 351704596)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.18 , pp. 5795-5802
    • Huang, H.1    Milojevic, J.2    Melacini, G.3
  • 35
    • 0031668862 scopus 로고    scopus 로고
    • Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes
    • DOI 10.1016/S0168-0102(98)00055-8, PII S0168010298000558
    • Abe, K., and Saito, H. (1998) Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes. Neurosci. Res. 31, 295-305 (Pubitemid 28446012)
    • (1998) Neuroscience Research , vol.31 , Issue.4 , pp. 295-305
    • Abe, K.1    Saito, H.2
  • 37
    • 77955819967 scopus 로고    scopus 로고
    • Kinetics of amyloid β monomer-to-oligomer exchange by NMR relaxation
    • Fawzi, N. L., Ying, J., Torchia, D. A., and Clore, G. M. (2010) Kinetics of amyloid β monomer-to-oligomer exchange by NMR relaxation. J. Am. Chem. Soc. 132, 9948-9951
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9948-9951
    • Fawzi, N.L.1    Ying, J.2    Torchia, D.A.3    Clore, G.M.4
  • 38
    • 0028872558 scopus 로고
    • Apolipoprotein e is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • Evans, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., and Lansbury, P. T., Jr. (1995) Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 92, 763-767
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury Jr., P.T.5
  • 39
    • 33847051684 scopus 로고    scopus 로고
    • Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Aβ interaction
    • Yan, Y., Liu, Y., Sorci, M., Belfort, G., Lustbader, J. W., Yan, S. S., and Wang, C. (2007) Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Aβ interaction. Biochemistry 46, 1724-1731
    • (2007) Biochemistry , vol.46 , pp. 1724-1731
    • Yan, Y.1    Liu, Y.2    Sorci, M.3    Belfort, G.4    Lustbader, J.W.5    Yan, S.S.6    Wang, C.7
  • 40
    • 78349309658 scopus 로고    scopus 로고
    • Mechanism of fiber assembly: Treatment of Aβ peptide aggregation with a coarse-grained united-residue force field
    • Rojas, A., Liwo, A., Browne, D., and Scheraga, H. A. (2010) Mechanism of fiber assembly: Treatment of Aβ peptide aggregation with a coarse-grained united-residue force field. J. Mol. Biol. 404, 537-552
    • (2010) J. Mol. Biol. , vol.404 , pp. 537-552
    • Rojas, A.1    Liwo, A.2    Browne, D.3    Scheraga, H.A.4
  • 42
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of α-synuclein and disaggregates existing fibrils
    • DOI 10.1074/jbc.M403129200
    • Zhu, M., Rajamani, S., Kaylor, J., Han, S., Zhou, F., and Fink, A. L. (2004) The flavonoid baicalein inhibits fibrillation of α-synuclein and disaggregates existing fibrils. J. Biol. Chem. 279, 26846-26857 (Pubitemid 38812518)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 43
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • DOI 10.1126/science.1063522
    • Conway, K. A., Rochet, J. C., Bieganski, R. M., and Lansbury, P. T., Jr. (2001) Kinetic stabilization of the α-synuclein protofibril by a dopamine- α-synuclein adduct. Science 294, 1346-1349 (Pubitemid 33063102)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.-C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 45
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 46
    • 0034042406 scopus 로고    scopus 로고
    • Synaptic plasticity and memory: An evaluation of the hypothesis
    • DOI 10.1146/annurev.neuro.23.1.649
    • Martin, S. J., Grimwood, P. D., and Morris, R. G. (2000) Synaptic plasticity and memory: An evaluation of the hypothesis. Annu. Rev. Neurosci. 23, 649-711 (Pubitemid 30350057)
    • (2000) Annual Review of Neuroscience , vol.23 , pp. 649-711
    • Martin, S.J.1    Grimwood, P.D.2    Morris, R.G.M.3
  • 48
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long term depression by disrupting neuronal glutamate uptake
    • Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., and Selkoe, D. (2009) Soluble oligomers of amyloid β protein facilitate hippocampal long term depression by disrupting neuronal glutamate uptake. Neuron 62, 788-801
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 50
    • 0030747399 scopus 로고    scopus 로고
    • Biological effects of myricetin
    • DOI 10.1016/S0306-3623(96)00421-1, PII S0306362396004211
    • Ong, K. C., and Khoo, H. E. (1997) Biological effects of myricetin. Gen. Pharmacol. 29, 121-126 (Pubitemid 27312361)
    • (1997) General Pharmacology , vol.29 , Issue.2 , pp. 121-126
    • Ong, K.C.1    Khoo, H.-E.2
  • 51
    • 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., and Sugimoto, H. (2008) 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 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
  • 52
    • 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
    • DOI 10.1111/j.1471-4159.2004.02899.x
    • Sultana, R., Ravagna, A., Mohmmad-Abdul, H., Calabrese, V., and Butterfield, D. A. (2005) Ferulic acid ethyl ester protects neurons against amyloid β peptide(1-42)-induced oxidative stress and neurotoxicity: Relationship to antioxidant activity. J. Neurochem. 92, 749-758 (Pubitemid 40229546)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.4 , pp. 749-758
    • Sultana, R.1    Ravagna, A.2    Mohmmad-Abdul, H.3    Calabrese, V.4    Butterfield, D.A.5
  • 53
    • 78650403081 scopus 로고    scopus 로고
    • Reimagining Alzheimer disease-an age-based hypothesis
    • Herrup, K. (2010) Reimagining Alzheimer disease-an age-based hypothesis. J. Neurosci. 30, 16755-16762
    • (2010) J. Neurosci. , vol.30 , pp. 16755-16762
    • Herrup, K.1
  • 54
    • 78049512483 scopus 로고    scopus 로고
    • Novel approaches for analyzing gut microbes and dietary polyphenols: Challenges and opportunities
    • Kemperman, R. A., Bolca, S., Roger, L. C., and Vaughan, E. E. (2010) Novel approaches for analyzing gut microbes and dietary polyphenols: Challenges and opportunities. Microbiology 156, 3224-3231
    • (2010) Microbiology , vol.156 , pp. 3224-3231
    • Kemperman, R.A.1    Bolca, S.2    Roger, L.C.3    Vaughan, E.E.4


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