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Volumn 14, Issue 6, 2013, Pages 12411-12457

Protein folding and aggregation into amyloid: The interference by natural phenolic compounds

Author keywords

Amyloid; Amyloid aggregation; Natural phenols; Polyphenols

Indexed keywords

AMYLOID; CURCUMIN; EPIGALLOCATECHIN GALLATE; FERULIC ACID; GELATINASE B; MYRICETIN; NORDIHYDROGUAIARETIC ACID; OLEUROPEIN; OLIVE OIL; PICEATANNOL; QUERCETIN; RESVERATROL; ROSMARINIC ACID; SERUM AMYLOID A; BIOLOGICAL PRODUCT; PHENOL DERIVATIVE;

EID: 84888406392     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms140612411     Document Type: Review
Times cited : (180)

References (332)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding
    • Levinthal, C. Are there pathways for protein folding? J. Chem. Phys. 1968, 85, 44-45.
    • (1968) J. Chem. Phys , vol.85 , pp. 44-45
    • Levinthal, C.1
  • 3
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M.; Dobson, C.M. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 81, 678-699.
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas, P.J.; Qu, B.-H.; Pedersen, P.L. Defective protein folding as a basis of human disease. Trends Biochem. Sci. 1995, 20, 456-459.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.-H.2    Pedersen, P.L.3
  • 6
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. Protein folding and misfolding. Nature 2003, 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 7
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D.J. Folding proteins in fatal ways. Nature 2003, 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 9
    • 29244450505 scopus 로고    scopus 로고
    • Partitioning conformational intermediates between competing refolding and aggregation pathways: Insights into transthyretin amyloid disease
    • Wiseman, R.L.; Powers, E.T.; Kelly, J.W. Partitioning conformational intermediates between competing refolding and aggregation pathways: Insights into transthyretin amyloid disease. Biochemistry 2005, 44, 16612-16623.
    • (2005) Biochemistry , vol.44 , pp. 16612-16623
    • Wiseman, R.L.1    Powers, E.T.2    Kelly, J.W.3
  • 10
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • Jahn, T.T.; Radford, S.E. Folding versus aggregation: Polypeptide conformations on competing pathways. Arch. Biochem. Biophys. 2008, 469, 100-117.
    • (2008) Arch. Biochem. Biophys , vol.469 , pp. 100-117
    • Jahn, T.T.1    Radford, S.E.2
  • 12
    • 84860859564 scopus 로고    scopus 로고
    • Modeling human neurodegenerative diseases in transgenic systems
    • Gama Sosa, M.A.; de Gasperi, R.; Elder, G.A. Modeling human neurodegenerative diseases in transgenic systems. Hum. Genet. 2012, 131, 535-563.
    • (2012) Hum. Genet , vol.131 , pp. 535-563
    • Gama Sosa, M.A.1    De Gasperi, R.2    Elder, G.A.3
  • 14
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neuronal death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • Perutz, M.F.; Windle, A.H. Cause of neuronal death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature 2001, 412, 143-144.
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 17
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M.; Klyubin, I.; Fadeeva, J.V.; Cullen, W.K.; Anwyl, R.; Wolfe, M.S.; Rowan, M.J.; Selkoe, D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 18
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization not fibrillization is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson’s disease. Implication for pathogenesis and therapy
    • Conway, K.A.; Lee, S.-J.; Rochet, J.C.; Ding, T.T.; Williamson, R.E.; Lansbury, P.T. Acceleration of oligomerization not fibrillization is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson’s disease. Implication for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA 2000, 97, 571-576.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.-J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 19
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach, N.; Deechingkit, S.; Jiang, X.; Kelly, J.W.; Buxbaum, J.N. Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc. Natl. Acad. Sci. USA 2004, 101, 2817-2822.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechingkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 21
    • 0034994097 scopus 로고    scopus 로고
    • Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis-associated amyloidosis
    • Hirakura, Y.; Kagan, B.L. Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis-associated amyloidosis. Amyloid 2001, 8, 94-100.
    • (2001) Amyloid , vol.8 , pp. 94-100
    • Hirakura, Y.1    Kagan, B.L.2
  • 22
    • 0036793927 scopus 로고    scopus 로고
    • Collagen XVIII: A novel heparan sulfate proteoglycan associated with vascular amyloid depositions and senile plaques in Alzheimer’s disease brains
    • Van Horssen, J.; Wilhelmus, M.M.; Heljasvaara, R.; Pihlajaniemi, T.; Wesseling, P.; de Waal, R.M.; Verbeek, M.M. Collagen XVIII: A novel heparan sulfate proteoglycan associated with vascular amyloid depositions and senile plaques in Alzheimer’s disease brains. Brain Pathol. 2002, 12, 456-462.
    • (2002) Brain Pathol , vol.12 , pp. 456-462
    • Van Horssen, J.1    Wilhelmus, M.M.2    Heljasvaara, R.3    Pihlajaniemi, T.4    Wesseling, P.5    De Waal, R.M.6    Verbeek, M.M.7
  • 23
    • 0035997236 scopus 로고    scopus 로고
    • Glycosaminoglycans and beta-amyloid, prion and tau peptides in neurodegenerative diseases
    • Diaz-Nido, J.; Wandosell, F.; Avila, J. Glycosaminoglycans and beta-amyloid, prion and tau peptides in neurodegenerative diseases. Peptides 2002, 23, 1323-1332.
    • (2002) Peptides , vol.23 , pp. 1323-1332
    • Diaz-Nido, J.1    Wandosell, F.2    Avila, J.3
  • 25
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • Walsh, D.M.; Selkoe, D.J. Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration. Protein Peptide Lett. 2004, 11, 1-16.
    • (2004) Protein Peptide Lett , vol.11 , pp. 1-16
    • Walsh, D.M.1    Selkoe, D.J.2
  • 27
    • 14644442872 scopus 로고    scopus 로고
    • Causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice
    • Billings, L.M.; Oddo, S.; Green, K.N.; McGaugh, J.L.; LaFerla, F.M. Intraneuronal Aβ causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice. Neuron 2005, 45, 675-688.
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    Laferla, F.M.5    Intraneuronal, A.Β.6
  • 30
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida, Y.; Kurosawa, M.; Nukina, N.; Ito, K.; Oda, T.; Tanaka, M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. USA 2009, 106, 9679-9684.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 32
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya, V.; Bocharova, O.V.; Bronstein, I.; Baskakov, I.V. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 2006, 281, 13828-13836.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 37
    • 35848951621 scopus 로고    scopus 로고
    • Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner
    • Chafekar, F.M.; Hoozemans, J.J.; Zwart, R.; Baas, F.; Scheper, W. Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antiox. Red. Signal. 2007, 9, 2245-2254.
    • (2007) Antiox. Red. Signal , vol.9 , pp. 2245-2254
    • Chafekar, F.M.1    Hoozemans, J.J.2    Zwart, R.3    Baas, F.4    Scheper, W.5
  • 42
    • 0029078972 scopus 로고
    • Correlation of synaptic and pathological markers with cognition of the elderly
    • Dickson, D.W. Correlation of synaptic and pathological markers with cognition of the elderly. Neurobiol. Aging 1995, 16, 285-298.
    • (1995) Neurobiol. Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1
  • 43
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks—A driver for protein function in evolution
    • Powers, E.T.; Balch, W.E. Diversity in the origins of proteostasis networks—A driver for protein function in evolution. Nat. Rev. Mol. Cell Biol. 2013, 14, 237-248.
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 45
    • 51849084313 scopus 로고    scopus 로고
    • Amylin proprotein proessing generates progressively more amyloidogenica peptides that initially sample the helical state
    • Yonemoto, I.T.; Kroon, G.J.; Dyson, H.J.; Balch, W.E.; Kelly, J.W. Amylin proprotein proessing generates progressively more amyloidogenica peptides that initially sample the helical state. Biochemistry 2008, 47, 9900-9910.
    • (2008) Biochemistry , vol.47 , pp. 9900-9910
    • Yonemoto, I.T.1    Kroon, G.J.2    Dyson, H.J.3    Balch, W.E.4    Kelly, J.W.5
  • 46
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon, W.; Kelly, J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992, 31, 8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 49
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer’s disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J.D.; Lansbury, P.T. Models of amyloid seeding in Alzheimer’s disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 1997, 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 50
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers—A novel pathway of amyloid formation
    • Modler, A.J.; Gast, K.; Lutsch, G.; Damaschun, G. Assembly of amyloid protofibrils via critical oligomers—A novel pathway of amyloid formation. J. Mol. Biol. 2003, 325, 135-148.
    • (2003) J. Mol. Biol , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 51
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
    • Gosal, W.S; Morten, L.J.; Hewitt, E.W.; Smith, D.A.; Thomson, N.H.; Radford, S.E. Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J. Mol. Biol. 2005, 351, 850-864.
    • (2005) J. Mol. Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, L.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 52
    • 33750294048 scopus 로고    scopus 로고
    • Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry
    • Smith, A.M.; Jahn, T.R.; Ashcroft, A.E.; Radford, S.E. Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J. Mol. Biol. 2006, 364, 9-19.
    • (2006) J. Mol. Biol , vol.364 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 55
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M.; Kayed, R.; Milton, S.; Glabe, C.G. Small molecule inhibitors of aggregation indicate that amyloid beta 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
  • 56
  • 57
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas, D.A.; Carrell, R.W. Serpinopathies and the conformational dementias. Nat. Rev. Genet. 2002, 3, 759-768.
    • (2002) Nat. Rev. Genet , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 59
    • 33744497267 scopus 로고    scopus 로고
    • Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I
    • Guo, Z.; Eisenberg, D. Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proc. Natl. Acad. Sci. USA 2006, 103, 8042-8047.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8042-8047
    • Guo, Z.1    Eisenberg, D.2
  • 61
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    • Plakoutsi, G.; Bemporad, F.; Calamai, M.; Taddei, N.; Dobson, C.M.; Chiti, F. Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 2005, 351, 910-922.
    • (2005) J. Mol. Biol , vol.351 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Calamai, M.3    Taddei, N.4    Dobson, C.M.5    Chiti, F.6
  • 62
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: A link between gene expression levels and aggregation rates of human proteins
    • Tartaglia, G.G.; Pechmann, S.; Dobson, C.M.; Vendruscolo, M. Life on the edge: A link between gene expression levels and aggregation rates of human proteins. Trends Biochem. Sci. 2007, 32, 204-206.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 63
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M.Y.; Goldberg, A.L. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron 2001, 29, 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 64
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia, R.; Braakman, I. Quality control in the endoplasmic reticulum protein factory. Nature 2003, 426, 891-894.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 66
    • 0028171547 scopus 로고
    • Ultrastructural analysis of beta-amyloid-induced apoptosis in cultured hippocampal neurons
    • Watt, J.A.; Pike, C.J.; Walencewicz-Wasserman, A.J.; Cotman, C.W. Ultrastructural analysis of beta-amyloid-induced apoptosis in cultured hippocampal neurons. Brain Res. 1994, 661, 147-156.
    • (1994) Brain Res , vol.661 , pp. 147-156
    • Watt, J.A.1    Pike, C.J.2    Walencewicz-Wasserman, A.J.3    Cotman, C.W.4
  • 68
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington’s disease and related disorders
    • Ross, C.A. Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington’s disease and related disorders. Neuron 2002, 35, 819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 69
    • 0032470007 scopus 로고    scopus 로고
    • The ultrastructural effects of beta-amyloid peptide on cultured PC12 cells: Changes in cytoplasmic and intramembranous features
    • Lane, N.J.; Balbo, A.; Fukuyama, R.; Rapoport, S.I.; Galdzick, Z. The ultrastructural effects of beta-amyloid peptide on cultured PC12 cells: Changes in cytoplasmic and intramembranous features. J. Neurocytol. 1998, 27, 707-718.
    • (1998) J. Neurocytol , vol.27 , pp. 707-718
    • Lane, N.J.1    Balbo, A.2    Fukuyama, R.3    Rapoport, S.I.4    Galdzick, Z.5
  • 70
    • 0035478618 scopus 로고    scopus 로고
    • Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima, Y.; Gotoh, Y.; Zieg, J.; Barrett, T.; Takano, H.; Flavell, R.; Davis, R.J.; Shirasaki, Y.; Greenberg, M.E. Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J. Neurosci. 2001, 21, 7551-7560.
    • (2001) J. Neurosci. , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 71
    • 0034853813 scopus 로고    scopus 로고
    • Ultrastructure evidence of necrotic neural cell death in familial Alzheimer’s disease brains bearing presenilin-1 E280A mutation
    • Velez-Pardo, C.; Arroyave, S.T.; Lopera, F.; Castano, A.D.; Jimenez Del Rio, M. Ultrastructure evidence of necrotic neural cell death in familial Alzheimer’s disease brains bearing presenilin-1 E280A mutation. J. Alzheimers Dis. 2001, 3, 409-415.
    • (2001) J. Alzheimers Dis , vol.3 , pp. 409-415
    • Velez-Pardo, C.1    Arroyave, S.T.2    Lopera, F.3    Castano, A.D.4    Jimenez Del Rio, M.5
  • 72
    • 84874597155 scopus 로고    scopus 로고
    • Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model
    • Eremenko, E.; Ben-Zvi, A.; Morozova-Roche, L.A.; Raveh, D. Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model. PLoS One 2013, 8, e58218.
    • (2013) Plos One , vol.8
    • Eremenko, E.1    Ben-Zvi, A.2    Morozova-Roche, L.A.3    Raveh, D.4
  • 74
    • 84876374851 scopus 로고    scopus 로고
    • Fattoretti, P. Early selective vulnerability of synapses and synaptic mitochondria in the hippocampal CA1 region of the Tg2576 mouse model of Alzheimer’s disease
    • Balietti, M.; Giorgetti, B.; Casoli, T.; Solazzi, M.; Tamagnini, F.; Burattini, C.; Aicardi, G.; Fattoretti, P. Early selective vulnerability of synapses and synaptic mitochondria in the hippocampal CA1 region of the Tg2576 mouse model of Alzheimer’s disease. J. Alzheimers Dis. 2013, 34, 887-896.
    • (2013) J. Alzheimers Dis , vol.34 , pp. 887-896
    • Balietti, M.1    Giorgetti, B.2    Casoli, T.3    Solazzi, M.4    Tamagnini, F.5    Burattini, C.6    Aicardi, G.7
  • 75
    • 84874303866 scopus 로고    scopus 로고
    • Impaired transcription in Alzheimer’s disease: Key role in mitochondrial dysfunction and oxidative stress
    • Caldeira, G.L.; Ferreira, I.L.; Rego, A.C. Impaired transcription in Alzheimer’s disease: Key role in mitochondrial dysfunction and oxidative stress. J. Alzheimers Dis. 2013, 34, 115-131.
    • (2013) J. Alzheimers Dis , vol.34 , pp. 115-131
    • Caldeira, G.L.1    Ferreira, I.L.2    Rego, A.C.3
  • 76
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzeimer’s disease brain: Central role for amyloid β-peptide
    • Butterfield, A.D.; Drake, J.; Pocernich, C.; Castegna, A. Evidence of oxidative damage in Alzeimer’s disease brain: Central role for amyloid β-peptide. Trends Mol. Med. 2001, 7, 548-554.
    • (2001) Trends Mol. Med. , vol.7 , pp. 548-554
    • Butterfield, A.D.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 78
    • 84864622023 scopus 로고    scopus 로고
    • Study of neurotoxic intracellular calcium signalling triggered by amyloids
    • Villalobos, C.; Caballero, E.; Sanz-Blasco, S.; Núñez, L. Study of neurotoxic intracellular calcium signalling triggered by amyloids. Methods Mol. Biol. 2012, 849, 289-302.
    • (2012) Methods Mol. Biol , vol.849 , pp. 289-302
    • Villalobos, C.1    Caballero, E.2    Sanz-Blasco, S.3    Núñez, L.4
  • 79
    • 0034858202 scopus 로고    scopus 로고
    • Mechanisms of amyloid β protein-induced modification in ion transport systems: Implications for neurodegenerative diseases
    • Kourie, J.I. Mechanisms of amyloid β protein-induced modification in ion transport systems: Implications for neurodegenerative diseases. Cell. Mol. Neurobiol. 2001, 21, 173-213.
    • (2001) Cell. Mol. Neurobiol , vol.21 , pp. 173-213
    • Kourie, J.I.1
  • 80
    • 84877030960 scopus 로고    scopus 로고
    • Vascular oxidative stress and mitochondrial failure in the pathobiology of Alzheimer’s disease: New approach to therapy
    • press
    • Sochocka, M.; Koutsouraki, E.S.; Gąsiorowski, K.; Leszek, J. Vascular oxidative stress and mitochondrial failure in the pathobiology of Alzheimer’s disease: New approach to therapy. CNS Neurol. Disord. Drug Targets 2013, in press.
    • (2013) CNS Neurol. Disord. Drug Targets
    • Sochocka, M.1    Koutsouraki, E.S.2    Gąsiorowski, K.3    Leszek, J.4
  • 81
    • 0036124813 scopus 로고    scopus 로고
    • Oxidative stress and the prion protein in transmissible spongiform encephalopathies
    • Milhavet, O.; Lehmann, S. Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res. Rev. 2002, 38, 328-339.
    • (2002) Brain Res. Rev , vol.38 , pp. 328-339
    • Milhavet, O.1    Lehmann, S.2
  • 82
    • 84877072330 scopus 로고    scopus 로고
    • Amyloid β-peptide (1-42)-induced oxidative stress in Alzheimer disease: Importance in disease pathogenesis and progression
    • press
    • Butterfield, D.A.; Swomley, A.M.; Sultana, R. Amyloid β-peptide (1-42)-induced oxidative stress in Alzheimer disease: Importance in disease pathogenesis and progression. Antioxid. Redox Signal. 2013, in press.
    • (2013) Antioxid. Redox Signal
    • Butterfield, D.A.1    Swomley, A.M.2    Sultana, R.3
  • 83
    • 0035955513 scopus 로고    scopus 로고
    • α-Lipoic acid protects rat cortical neurons against cell death induced by amyloid and hydrogen peroxide through the Akt signalling pathway
    • Zhang, L.; Xing, G.Q.; Barker, J.L.; Chang, Y.; Maric, D.; Ma, W.; Li, B.-S.; Rubinow, D.R. α-Lipoic acid protects rat cortical neurons against cell death induced by amyloid and hydrogen peroxide through the Akt signalling pathway. Neurosci. Lett. 2001, 312, 125-128.
    • (2001) Neurosci. Lett , vol.312 , pp. 125-128
    • Zhang, L.1    Xing, G.Q.2    Barker, J.L.3    Chang, Y.4    Maric, D.5    Ma, W.6    Li, B.-S.7    Rubinow, D.R.8
  • 84
    • 78649634550 scopus 로고    scopus 로고
    • α-Tocopherol quinone inhibits β-amyloid aggregation and cytotoxicity, disaggregates preformed fibrils and decreases the production of reactive oxygen species, NO and inflammatory cytokines
    • Yang, S.G.; Wang, W.Y.; Ling, T.J.; Feng, Y.; Du, X.T.; Zhang, X.; Sun, X.X.; Zhao, M.; Xue, D.; Yang, Y. et al. α-Tocopherol quinone inhibits β-amyloid aggregation and cytotoxicity, disaggregates preformed fibrils and decreases the production of reactive oxygen species, NO and inflammatory cytokines. Neurochem. Int. 2010, 57, 914-922.
    • (2010) Neurochem. Int , vol.57 , pp. 914-922
    • Yang, S.G.1    Wang, W.Y.2    Ling, T.J.3    Feng, Y.4    Du, X.T.5    Zhang, X.6    Sun, X.X.7    Zhao, M.8    Xue, D.9    Yang, Y.10
  • 86
    • 84856623196 scopus 로고    scopus 로고
    • Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer’s disease
    • Choi, D.Y.; Lee, Y.J.; Hong, J.T.; Lee, H.J. Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer’s disease. Brain Res. Bull. 2012, 87, 144-153.
    • (2012) Brain Res. Bull. , vol.87 , pp. 144-153
    • Choi, D.Y.1    Lee, Y.J.2    Hong, J.T.3    Lee, H.J.4
  • 88
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • Keller, J.N.; Huang, F.F.; Markesbery, W.R. Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 2002, 98, 149-156.
    • (2002) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 89
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers
    • Fratta, P.; Engel, W.K.; McFerrin, J.; Davies, K.J.; Lin, S.W.; Askanas, V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am. J. Pathol. 2005, 167, 517-526.
    • (2005) Am. J. Pathol , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.4    Lin, S.W.5    Askanas, V.6
  • 90
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by Huntingtin
    • Wyttenbach, A.; Sauvageot, O.; Carmichael, J.; Diaz-Latoud, C.; Arrigo, A.-P.; Rubinsztein, D.C. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by Huntingtin. Hum. Mol. Genet. 2002, 11, 1137-1151.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.-P.5    Rubinsztein, D.C.6
  • 91
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington’s disease
    • Wyttenbach, A.; Swartz, J.; Kita, H.; Thykjaer, T.; Carmichael, J.; Bradley, J.; Brown, R.; Maxwell, M.; Schapira, A.; Orntoft, T.F. et al. Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington’s disease. Hum. Mol. Genet. 2001, 10, 1829-1845.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3    Thykjaer, T.4    Carmichael, J.5    Bradley, J.6    Brown, R.7    Maxwell, M.8    Schapira, A.9    Orntoft, T.F.10
  • 92
    • 0036669345 scopus 로고    scopus 로고
    • The radical model of Alzheimer’s disease: Specific recognition of Gly29 and Gly33 by Met35 in a beta-sheet model of Abeta: An ONIOM study
    • Brunelle, P.; Rauk, A. The radical model of Alzheimer’s disease: Specific recognition of Gly29 and Gly33 by Met35 in a beta-sheet model of Abeta: An ONIOM study. J. Alzheimers Dis. 2002, 4, 283-289.
    • (2002) J. Alzheimers Dis , vol.4 , pp. 283-289
    • Brunelle, P.1    Rauk, A.2
  • 93
    • 0036182026 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson’s disease
    • Orth, M.; Shapira, A.H.V. Mitochondrial involvement in Parkinson’s disease. Neurochem. Int. 2002, 40, 533-541.
    • (2002) Neurochem. Int , vol.40 , pp. 533-541
    • Orth, M.1    Shapira, A.H.V.2
  • 94
    • 0035873812 scopus 로고    scopus 로고
    • α-Synuclein implicated in Parkinson’s disease catalyzes the formation of hydrogen peroxide in vitro
    • Turnbull, S.; Tabner, B.J.; El-Agnaf, O.M.A.; Moore, S.; Davies, Y.; Allsop, D. α-Synuclein implicated in Parkinson’s disease catalyzes the formation of hydrogen peroxide in vitro. Free Rad. Biol. Med. 2001, 30, 1163-1170.
    • (2001) Free Rad. Biol. Med , vol.30 , pp. 1163-1170
    • Turnbull, S.1    Tabner, B.J.2    El-Agnaf, O.M.A.3    Moore, S.4    Davies, Y.5    Allsop, D.6
  • 95
    • 0036591852 scopus 로고    scopus 로고
    • Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer’s disease and Parkinson’s disease
    • Tabner, B.J.; Turnbull, S.; El-Agnaf, O.M.A.; Allsop, D. Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer’s disease and Parkinson’s disease. Free Rad. Biol. Med. 2002, 32, 1076-1083.
    • (2002) Free Rad. Biol. Med , vol.32 , pp. 1076-1083
    • Tabner, B.J.1    Turnbull, S.2    El-Agnaf, O.M.A.3    Allsop, D.4
  • 97
    • 0036845314 scopus 로고    scopus 로고
    • Microglia enhance β-amyloid peptide-induced toxicity in cortical and mesencephalic neurons by producing reactive oxygen species
    • Qin, L.; Liu, Y.; Cooper, C.; Liu, B.; Wilson, B.; Hong, J.-S. Microglia enhance β-amyloid peptide-induced toxicity in cortical and mesencephalic neurons by producing reactive oxygen species. J. Neurochem. 2002, 83, 973-983.
    • (2002) J. Neurochem , vol.83 , pp. 973-983
    • Qin, L.1    Liu, Y.2    Cooper, C.3    Liu, B.4    Wilson, B.5    Hong, J.-S.6
  • 98
    • 0032883766 scopus 로고    scopus 로고
    • Impairment of membrane transport and signal transduction systems by amyloidogenic proteins
    • Mattson, M.P. Impairment of membrane transport and signal transduction systems by amyloidogenic proteins. Methods Enzymol. 1999, 309, 733-768.
    • (1999) Methods Enzymol , vol.309 , pp. 733-768
    • Mattson, M.P.1
  • 99
    • 0037100213 scopus 로고    scopus 로고
    • Effect of amyloid beta-peptide on permeability transition pore: A comparative study
    • Moreira, P.I.; Santos, M.S.; Moreno, A.; Rego, A.C.; Oliveira, C. Effect of amyloid beta-peptide on permeability transition pore: A comparative study. J. Neurosci. Res. 2002, 15, 257-267.
    • (2002) J. Neurosci. Res , vol.15 , pp. 257-267
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Rego, A.C.4    Oliveira, C.5
  • 100
    • 72149118206 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore in Alzheimer's disease: Cyclophilin D and amyloid beta
    • Du, H.; Yan, S.S. Mitochondrial permeability transition pore in Alzheimer's disease: Cyclophilin D and amyloid beta. Biochim. Biophys. Acta 2010, 1802, 198-204.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 198-204
    • Du, H.1    Yan, S.S.2
  • 101
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier, T.C. Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 2001, 36, 1539-1550.
    • (2001) Exp. Gerontol , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 102
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer’s β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevation by a common mechanism in a hypopthalamic GnRH neuronal cell line
    • Kawahara, M.; Kuroda, Y.; Arispe, N.; Rojas, E. Alzheimer’s β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevation by a common mechanism in a hypopthalamic GnRH neuronal cell line. J. Biol. Chem. 2000, 275, 14077-14083.
    • (2000) J. Biol. Chem , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 103
    • 1842529223 scopus 로고    scopus 로고
    • Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F
    • Sirangelo, I.; Malmo, C.; Iannuzzi, C.; Mezzogiorno, A.; Bianco, M.R.; Papa, M.; Irace, G. Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F. J. Biol. Chem. 2004, 279, 13183-13189.
    • (2004) J. Biol. Chem , vol.279 , pp. 13183-13189
    • Sirangelo, I.1    Malmo, C.2    Iannuzzi, C.3    Mezzogiorno, A.4    Bianco, M.R.5    Papa, M.6    Irace, G.7
  • 105
    • 24344467958 scopus 로고    scopus 로고
    • Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates
    • Cecchi, C.; Baglioni, S.; Fiorillo, C.; Pensalfini, A.; Liguri, G.; Nosi, D.; Rigacci, S.; Bucciantini, M.; Stefani, M. Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates. J. Cell Sci. 2005, 118, 3459-3470.
    • (2005) J. Cell Sci , vol.118 , pp. 3459-3470
    • Cecchi, C.1    Baglioni, S.2    Fiorillo, C.3    Pensalfini, A.4    Liguri, G.5    Nosi, D.6    Rigacci, S.7    Bucciantini, M.8    Stefani, M.9
  • 106
    • 84864810728 scopus 로고    scopus 로고
    • Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers
    • Evangelisti, E.; Cecchi, C.; Cascella, R.; Sgromo, C.; Liguri, G.; Dobson, C.M.; Chiti, F.; Stefani, M. Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers. J. Cell Sci. 2012, 125, 2416-2427.
    • (2012) J. Cell Sci , vol.125 , pp. 2416-2427
    • Evangelisti, E.1    Cecchi, C.2    Cascella, R.3    Sgromo, C.4    Liguri, G.5    Dobson, C.M.6    Chiti, F.7    Stefani, M.8
  • 107
    • 33845661843 scopus 로고    scopus 로고
    • Aβ induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597-624)
    • Shadek, G.M.; Kummer, M.P.; Lu, D.C.; Galvan, V.; Bredesen, D.E.; Koo, E.H. Aβ induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597-624). FASEB J. 2006, 20, 1254-1266.
    • (2006) FASEB J , vol.20 , pp. 1254-1266
    • Shadek, G.M.1    Kummer, M.P.2    Lu, D.C.3    Galvan, V.4    Bredesen, D.E.5    Koo, E.H.6
  • 108
    • 1242274383 scopus 로고    scopus 로고
    • Tumor necrosis factor death receptor signaling cascade Is required for amyloid-β protein-induced neuron death
    • He, P.; Zhong, Z.; Lindholm, K.; Berning, L.; Lee, W.; Lemere, C.; Staufenbiel, M.; Li, R.; Shen, Y. Tumor necrosis factor death receptor signaling cascade Is required for amyloid-β protein-induced neuron death. J. Neurosci. 2004, 24, 1760-1771.
    • (2004) J. Neurosci , vol.24 , pp. 1760-1771
    • He, P.1    Zhong, Z.2    Lindholm, K.3    Berning, L.4    Lee, W.5    Lemere, C.6    Staufenbiel, M.7    Li, R.8    Shen, Y.9
  • 109
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Laurén, J.; Gimbel, D.A.; Nygaard, H.B.; Gilbert, J.W.; Strittmatter, S.M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009, 457, 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 111
    • 0037189083 scopus 로고    scopus 로고
    • Advanced glycation end products (AGE) and their receptor (RAGE) in the brain of patients with Creutzfeldt-Jakob disease with prion plaques
    • Sasaki, N.; Takeuchi, M.; Chowei, H.; Kikuchi, S.; Hayashi, N.; Nakano, H.; Ikeda, S.; Yamagishi, T.; Kitamoto, T.; Saito, T. et al. Advanced glycation end products (AGE) and their receptor (RAGE) in the brain of patients with Creutzfeldt-Jakob disease with prion plaques. Neurosci. Lett. 2002, 326, 117-120.
    • (2002) Neurosci. Lett , vol.326 , pp. 117-120
    • Sasaki, N.1    Takeuchi, M.2    Chowei, H.3    Kikuchi, S.4    Hayashi, N.5    Nakano, H.6    Ikeda, S.7    Yamagishi, T.8    Kitamoto, T.9    Saito, T.10
  • 112
    • 33646925693 scopus 로고    scopus 로고
    • In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)
    • Monteiro, F.A.; Cardoso, I.; Mendes Sousa, M.; Saraiva, M.J. In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). FEBS Lett. 2006, 580, 3451-3456.
    • (2006) FEBS Lett , vol.580 , pp. 3451-3456
    • Monteiro, F.A.1    Cardoso, I.2    Mendes Sousa, M.3    Saraiva, M.J.4
  • 113
    • 84861050637 scopus 로고    scopus 로고
    • Is RAGE still a therapeutic target for Alzheimer’s disease?
    • Deane, R.J. Is RAGE still a therapeutic target for Alzheimer’s disease? Future Med. Chem. 2012, 4, 915-925.
    • (2012) Future Med. Chem , vol.4 , pp. 915-925
    • Deane, R.J.1
  • 114
    • 33745741894 scopus 로고    scopus 로고
    • Soluble receptor for advanced glycation end products: From disease marker to potential therapeutic target
    • Geroldi, D.; Falcone, C.; Emanuele, E. Soluble receptor for advanced glycation end products: From disease marker to potential therapeutic target. Curr. Med. Chem. 2006, 13, 1971-1978.
    • (2006) Curr. Med. Chem , vol.13 , pp. 1971-1978
    • Geroldi, D.1    Falcone, C.2    Emanuele, E.3
  • 116
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss
    • Hsieh, H.; Boehm, J.; Sato, C.; Iwatsubo, T.; Tomita, T.; Sisodia, S.; Malinow, R. AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss. Neuron 2006, 52, 831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 117
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice, F.G.; Velasco, P.T.; Lambert, M.P.; Viola, K.; Fernandez, S.J.; Ferreira, S.T.; Klein, W.L. Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J. Biol. Chem. 2007, 282, 11590-11601.
    • (2007) J. Biol. Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 118
    • 57649223693 scopus 로고    scopus 로고
    • Generic interaction of pre-fibrillar amyloid aggregates with NMDA and AMPA receptors results in free Ca2+ increase in primary neuronal cells
    • Pellistri, F.; Bucciantini, M.; Relini, A.; Gliozzi, A.; Robello, M.; Stefani, M. Generic interaction of pre-fibrillar amyloid aggregates with NMDA and AMPA receptors results in free Ca2+ increase in primary neuronal cells. J. Biol. Chem. 2008, 283, 29950-29960.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29950-29960
    • Pellistri, F.1    Bucciantini, M.2    Relini, A.3    Gliozzi, A.4    Robello, M.5    Stefani, M.6
  • 121
    • 13644271638 scopus 로고    scopus 로고
    • Cytotoxic and membrane perturbation effects of a novel amyloid forming model, peptide poly(Leucine-glutamic acid)
    • Jayakumar, R.; Jayaraman, M.; Koteeswarl, D.; Gomath, K. Cytotoxic and membrane perturbation effects of a novel amyloid forming model, peptide poly(leucine-glutamic acid). J. Biochem. 2004, 136, 457-462.
    • (2004) J. Biochem , vol.136 , pp. 457-462
    • Jayakumar, R.1    Jayaraman, M.2    Koteeswarl, D.3    Gomath, K.4
  • 122
  • 124
    • 84877689421 scopus 로고    scopus 로고
    • The β-sheet breakers and π-stacking
    • Jarmuła, A.; Stępkowski, D. The β-sheet breakers and π-stacking. J. Pept. Sci. 2013, doi:10.1002/psc.2506.
    • (2013) J. Pept. Sci
    • Jarmuła, A.1    Stępkowski, D.2
  • 126
    • 84873127460 scopus 로고    scopus 로고
    • A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1ΔE9 mouse model of Alzheimer’s disease
    • Parthsarathy, V.; McClean, P.L.; Hölscher, C.; Taylor, M.; Tinker, C.; Jones, G.; Kolosov, O.; Salvati, E.; Gregori, M.; Masserini, M. et al. A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1ΔE9 mouse model of Alzheimer’s disease. PLoS One 2013, 8, e54769.
    • (2013) Plos One , vol.8
    • Parthsarathy, V.1    McClean, P.L.2    Hölscher, C.3    Taylor, M.4    Tinker, C.5    Jones, G.6    Kolosov, O.7    Salvati, E.8    Gregori, M.9    Masserini, M.10
  • 127
    • 84857636679 scopus 로고    scopus 로고
    • Cyclic peptide inhibitor of apoC.II peptide fibril formation: Mechanistic indight from NMR and molecular dynamics analysis
    • Griffin, M.D.; Yeung, L.; Hung, A.; Todorova, N.; Mok, Y.F.; Karas, J.A.; Gooley, P.R.; Yarovsky, I.; Howlett, G.J. A cyclic peptide inhibitor of apoC.II peptide fibril formation: Mechanistic indight from NMR and molecular dynamics analysis. J. Mol. Biol. 2012, 416, 642-655.
    • (2012) J. Mol. Biol , vol.416 , pp. 642-655
    • Griffin, M.D.1    Yeung, L.2    Hung, A.3    Todorova, N.4    Mok, Y.F.5    Karas, J.A.6    Gooley, P.R.7    Yarovsky, I.8    Howlett, G.9
  • 128
    • 78951482692 scopus 로고    scopus 로고
    • Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue
    • Andreotti, G.; Vitale, R.M.; Avidan-Shpalter, C.; Amodeo, P.; Gazit, E.; Motta, A. Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue. J. Biol. Chem. 2011, 286, 2707-2718.
    • (2011) J. Biol. Chem , vol.286 , pp. 2707-2718
    • Andreotti, G.1    Vitale, R.M.2    Avidan-Shpalter, C.3    Amodeo, P.4    Gazit, E.5    Motta, A.6
  • 129
    • 36049022567 scopus 로고    scopus 로고
    • New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides
    • Soto, P.; Griffin, M.A.; Shea, J.E. New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides. Biophys. J. 2007, 93, 3015-3025.
    • (2007) Biophys. J , vol.93 , pp. 3015-3025
    • Soto, P.1    Griffin, M.A.2    Shea, J.E.3
  • 130
    • 82355164174 scopus 로고    scopus 로고
    • Testing the therapeutic potential of doxycycline in a Drosophila melanogaster model of Alzheimer disease
    • Costa, R.; Speretta, E.; Crowther, D.C.; Cardoso, I. Testing the therapeutic potential of doxycycline in a Drosophila melanogaster model of Alzheimer disease. J. Biol. Chem. 2011, 286, 41647-41655.
    • (2011) J. Biol. Chem , vol.286 , pp. 41647-41655
    • Costa, R.1    Speretta, E.2    Crowther, D.C.3    Cardoso, I.4
  • 134
    • 34250373347 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone
    • Lieu, V.H.; Wu, J.W.; Wang, S.S.; Wu, C.H. Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone. Biotechnol. Prog. 2007, 23, 698-706.
    • (2007) Biotechnol. Prog , vol.23 , pp. 698-706
    • Lieu, V.H.1    Wu, J.W.2    Wang, S.S.3    Wu, C.H.4
  • 135
    • 84875073880 scopus 로고    scopus 로고
    • Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: A structural and thermodynamic analysis
    • Sant’Anna, R.O.; Braga, C.A.; Polikarpov, I.; Ventura, S.; Lima, L.M.T.R.; Foguel, D. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: A structural and thermodynamic analysis. Int. J. Mol. Sci. 2013, 14, 5284-5311.
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 5284-5311
    • Sant’Anna, R.O.1    Braga, C.A.2    Polikarpov, I.3    Ventura, S.4    Lima, L.M.T.R.5    Foguel, D.6
  • 136
    • 0345862278 scopus 로고    scopus 로고
    • Effect of different anti-Abeta antibodies on Abeta fibrillogenesis as assessed by atomic force microscopy
    • Legleiter, J.; Czilli, D.L.; Gitter, B.; DeMattos, R.B.; Holtzman, D.M.; Kowalewski, T. Effect of different anti-Abeta antibodies on Abeta fibrillogenesis as assessed by atomic force microscopy. J. Mol. Biol. 2004, 335, 997-1006.
    • (2004) J. Mol. Biol , vol.335 , pp. 997-1006
    • Legleiter, J.1    Czilli, D.L.2    Gitter, B.3    Demattos, R.B.4    Holtzman, D.M.5    Kowalewski, T.6
  • 137
    • 84878321355 scopus 로고    scopus 로고
    • Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein
    • Abe, M.; Abe, Y.; Ohkuri, T.; Mishima, T.; Monji, A.; Kanba, S.; Ueda T. Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein. Protein Sci. 2013, 22, 467-474.
    • (2013) Protein Sci , vol.22 , pp. 467-474
    • Abe, M.1    Abe, Y.2    Ohkuri, T.3    Mishima, T.4    Monji, A.5    Kanba, S.6    Ueda, T.7
  • 138
    • 78249258414 scopus 로고    scopus 로고
    • Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: Effect of tetracycline and trehalose
    • Sirangelo, I.; Irace, G. Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: Effect of tetracycline and trehalose. Expert Opin. Ther. Targets 2010, 14, 1311-1321.
    • (2010) Expert Opin. Ther. Targets , vol.14 , pp. 1311-1321
    • Sirangelo, I.1    Irace, G.2
  • 140
    • 67651149466 scopus 로고    scopus 로고
    • Poloxamer 188 copolymer membrane sealant rescues toxicity of amyloid oligomers in vitro
    • Mina, E.W.; Lasagna-Reeves, C.; Glabe, C.G.; Kayed, R. Poloxamer 188 copolymer membrane sealant rescues toxicity of amyloid oligomers in vitro. J. Mol. Biol. 2009, 391, 577-585.
    • (2009) J. Mol. Biol , vol.391 , pp. 577-585
    • Mina, E.W.1    Lasagna-Reeves, C.2    Glabe, C.G.3    Kayed, R.4
  • 141
    • 68549085272 scopus 로고    scopus 로고
    • Molecular insight into the inhibition effect of trehalose on the nucleation and elongation of amyloid beta-peptide oligomers
    • Liu, F.F.; Ji, L.; Dong, X.Y.; Sun, Y. Molecular insight into the inhibition effect of trehalose on the nucleation and elongation of amyloid beta-peptide oligomers. J. Phys. Chem. B 2009, 113, 11320-11329.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11320-11329
    • Liu, F.F.1    Ji, L.2    Dong, X.Y.3    Sun, Y.4
  • 142
    • 36749011905 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action
    • Morshedi, D.; Rezaei-Ghaleh, N.; Ebrahim-Habibi, A.; Ahmadian, S.; Nemat-Gorgani, M. Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action. FEBS J. 2007, 274, 6415-6425.
    • (2007) FEBS J , vol.274 , pp. 6415-6425
    • Morshedi, D.1    Rezaei-Ghaleh, N.2    Ebrahim-Habibi, A.3    Ahmadian, S.4    Nemat-Gorgani, M.5
  • 143
    • 33748286734 scopus 로고    scopus 로고
    • Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH
    • Yang, F. Jr; Zhang, M.; Zhou, B.R.; Chen, J.; Liang, Y. Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH. J. Mol. Biol. 2006, 362, 821-834.
    • (2006) J. Mol. Biol , vol.362 , pp. 821-834
    • Yang, F.1    Zhang, M.2    Zhou, B.R.3    Chen, J.4    Liang, Y.5
  • 146
    • 79954571967 scopus 로고    scopus 로고
    • Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan
    • Alavez, S.; Vantipalli, M.C.; Zucker, D.J.S.; Klang, I.M.; Lithgrow, G.J. Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan. Nature 2011, 472, 226-229.
    • (2011) Nature , vol.472 , pp. 226-229
    • Alavez, S.1    Vantipalli, M.C.2    Zucker, D.J.S.3    Klang, I.M.4    Lithgrow, G.J.5
  • 147
    • 84871905647 scopus 로고    scopus 로고
    • Neuroprotection by cyclodextrin in cell and mouse models of Alzheimer disease
    • Yao, J.; Ho, D.; Calingasan, N.Y.; Pipalia, N.H.; Lin, M.T.; Beal, M.F. Neuroprotection by cyclodextrin in cell and mouse models of Alzheimer disease. J. Exp. Med. 2012, 209, 2501-2513.
    • (2012) J. Exp. Med. , vol.209 , pp. 2501-2513
    • Yao, J.1    Ho, D.2    Calingasan, N.Y.3    Pipalia, N.H.4    Lin, M.T.5    Beal, M.F.6
  • 148
    • 84856191510 scopus 로고    scopus 로고
    • The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate
    • Cabaleiro-Lago, C.; Szczepankiewicz, O.; Linse, S. The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate. Langmuir 2012, 28, 1852-1857.
    • (2012) Langmuir , vol.28 , pp. 1852-1857
    • Cabaleiro-Lago, C.1    Szczepankiewicz, O.2    Linse, S.3
  • 149
    • 77749320957 scopus 로고    scopus 로고
    • Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles
    • Cabaleiro-Lago, C.; Lynch, I.; Dawson, K.A.; Linse, S. Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles. Langmuir 2010, 26, 3453-3461.
    • (2010) Langmuir , vol.26 , pp. 3453-3461
    • Cabaleiro-Lago, C.1    Lynch, I.2    Dawson, K.A.3    Linse, S.4
  • 150
    • 33750052628 scopus 로고    scopus 로고
    • PEGylated phospholipid nanomicelles interact with beta-amyloid(1-42) and mitigate its beta-sheet formation, aggregation and neurotoxicity in vitro
    • Pai, A.S.; Rubinstein, I.; Onyüksel, H. PEGylated phospholipid nanomicelles interact with beta-amyloid(1-42) and mitigate its beta-sheet formation, aggregation and neurotoxicity in vitro. Peptides 2006, 27, 2858-2866.
    • (2006) Peptides , vol.27 , pp. 2858-2866
    • Pai, A.S.1    Rubinstein, I.2    Onyüksel, H.3
  • 151
    • 25144471718 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of beta-amyloid peptides via the amphiphilic surfactants
    • Wang, S.S.; Chen, Y.T.; Chou, S.W. Inhibition of amyloid fibril formation of beta-amyloid peptides via the amphiphilic surfactants. Biochim. Biophys. Acta 2005, 1741, 307-313.
    • (2005) Biochim. Biophys. Acta , vol.1741 , pp. 307-313
    • Wang, S.S.1    Chen, Y.T.2    Chou, S.W.3
  • 159
    • 84864931018 scopus 로고    scopus 로고
    • Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin
    • Almeida, M.R.; Saraiva, M.J. Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin. FEBS Lett. 2012, 586, 2891-2896.
    • (2012) FEBS Lett. , vol.586 , pp. 2891-2896
    • Almeida, M.R.1    Saraiva, M.J.2
  • 163
    • 79955865565 scopus 로고    scopus 로고
    • Monoclonal antibodies against β-amyloid (Aβ) for the treatment of Alzheimer’s disease: The Aβ target at a crossroads
    • Panza, F.; Frisardi, V.; Imbimbo, B.P.; Seripa, D.; Solfrizzi, V.; Pilotto, A. Monoclonal antibodies against β-amyloid (Aβ) for the treatment of Alzheimer’s disease: The Aβ target at a crossroads. Expert Opin. Biol. Ther. 2011, 11, 679-686.
    • (2011) Expert Opin. Biol. Ther. , vol.11 , pp. 679-686
    • Panza, F.1    Frisardi, V.2    Imbimbo, B.P.3    Seripa, D.4    Solfrizzi, V.5    Pilotto, A.6
  • 164
    • 84864976166 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer disease: The challenge of adverse effects
    • Liu, Y.H.; Giunta, B.; Zhou, H.D.; Tan, J.; Wang, Y.J. Immunotherapy for Alzheimer disease: The challenge of adverse effects. Nat. Rev. Neurol. 2012, 8, 465-469.
    • (2012) Nat. Rev. Neurol , vol.8 , pp. 465-469
    • Liu, Y.H.1    Giunta, B.2    Zhou, H.D.3    Tan, J.4    Wang, Y.J.5
  • 165
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern, S.L.; Caselli, E.; Grigorieff, N.; Shoichet, B.K. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J. Med. Chem. 2002, 45, 1712-1722.
    • (2002) J. Med. Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 167
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • Zhu, M.; Rajamani, S.; Kaylor, J.; Han, S.; Zhou, F.; Fink, A.L. The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils. J. Biol. Chem. 2004, 279, 26846-26857.
    • (2004) J. Biol. Chem , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 168
    • 5144220474 scopus 로고    scopus 로고
    • Efficient reversal of Alzheimer’s disease fibril formation and elimination of neurotoxicity by a small molecule
    • Blanchard, B.J.; Chen, A.; Rozeboom, L.M.; Stafford, K.A.; Weigele, P.; Ingram, V.M. Efficient reversal of Alzheimer’s disease fibril formation and elimination of neurotoxicity by a small molecule. Proc. Natl. Acad. Sci. USA 2004, 101, 14326-14332.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14326-14332
    • Blanchard, B.J.1    Chen, A.2    Rozeboom, L.M.3    Stafford, K.A.4    Weigele, P.5    Ingram, V.M.6
  • 169
    • 84868592337 scopus 로고    scopus 로고
    • Dietary curcumin counteracts extracellular transthyretin deposition: Insights on the mechanism of amyloid inhibition
    • Ferreira, N.; Santos, S.A.O.; Domingues, M.R.M.; Saraiva, M.J.; Almeida, M.R. Dietary curcumin counteracts extracellular transthyretin deposition: Insights on the mechanism of amyloid inhibition. Biochim. Biophys. Acta 2013, 1832, 39-45.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 39-45
    • Ferreira, N.1    Santos, S.A.O.2    Domingues, M.R.M.3    Saraiva, M.J.4    Almeida, M.R.5
  • 170
    • 84855650426 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidoses: ―In vivo‖ evidence from FAP mice models
    • Ferreira, N.; Saraiva, M.J.; Almeida, M.R. Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidoses: ―In vivo‖ evidence from FAP mice models. PLoS One 2012, 7, e29933.
    • (2012) Plos One , vol.7
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 173
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways
    • Ladiwala, A.R.A.; Dordick, J.S.; Tessier, P.M. Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways. J. Biol. Chem. 2011, 286, 3209-3218.
    • (2011) J. Biol. Chem , vol.286 , pp. 3209-3218
    • Ladiwala, A.R.A.1    Dordick, J.S.2    Tessier, P.M.3
  • 174
    • 79960501434 scopus 로고    scopus 로고
    • Polyphenolic glycosides and aglycones utilize opposing pathways to selectively remodel and inactivate toxic oligomers of amyloid β
    • Ladiwala, A.R.A.; Mora-Pale, M.M.; Lin, J.C.; Bale, S.S.; Fishman, Z.S.; Dordick, J.S.; Tessier, P.M. Polyphenolic glycosides and aglycones utilize opposing pathways to selectively remodel and inactivate toxic oligomers of amyloid β. Chembiochem 2011, 12, 1749-1758.
    • (2011) Chembiochem , vol.12 , pp. 1749-1758
    • Ladiwala, A.R.A.1    Mora-Pale, M.M.2    Lin, J.C.3    Bale, S.S.4    Fishman, Z.S.5    Dordick, J.S.6    Tessier, P.M.7
  • 178
    • 79951931265 scopus 로고    scopus 로고
    • Adherence to a Mediterranean-type dietary pattern and cognitive decline in a community population
    • Tangney, C.C.; Kwasny, M.J.; Li, H.; Wilson, R.S.; Evans, D.A.; Morris M.C. Adherence to a Mediterranean-type dietary pattern and cognitive decline in a community population. Am. J. Clin. Nutr. 2011, 93, 601-607.
    • (2011) Am. J. Clin. Nutr , vol.93 , pp. 601-607
    • Tangney, C.C.1    Kwasny, M.J.2    Li, H.3    Wilson, R.S.4    Evans, D.A.5    Morris, M.C.6
  • 183
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim, G.P.; Chu, T.; Yang, F.; Beech, W.; Frautschy, S.A.; Cole, G.M. 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
  • 184
    • 70349481513 scopus 로고    scopus 로고
    • The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
    • Hudson, S.A.; Ecroyd, H.; Kee, T.W.; Carver, J.A. The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds. FEBS J. 2009, 276, 5960-5972.
    • (2009) FEBS J , vol.276 , pp. 5960-5972
    • Hudson, S.A.1    Ecroyd, H.2    Kee, T.W.3    Carver, J.A.4
  • 185
    • 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
  • 186
    • 79960910835 scopus 로고    scopus 로고
    • Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
    • Ferreira, N.; Saraiva, M.J.; Almeida, M.R. Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS Lett. 2011, 585, 2424-2430.
    • (2011) FEBS Lett , vol.585 , pp. 2424-2430
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 188
    • 84856831983 scopus 로고    scopus 로고
    • Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic drosophila
    • Caesar, I.; Jonson, M.; Nilsson, K.P.R.; Thor, S.; Hammarström, P. Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic drosophila. PLoS One 2012, 7, e31424.
    • (2012) Plos One , vol.7
    • Caesar, I.1    Jonson, M.2    Nilsson, K.P.R.3    Thor, S.4    Hammarström, P.5
  • 189
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent Alzheimer’s pathology through different effects on the amyloid-β aggregation pathway
    • Hamaguchi, T.; Ono, K.; Murase, A.; Yamada, M. Phenolic compounds prevent Alzheimer’s pathology through different effects on the amyloid-β aggregation pathway. Am. J. Pathol. 2009, 175, 2557-2565.
    • (2009) Am. J. Pathol , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 190
    • 67849103420 scopus 로고    scopus 로고
    • Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme
    • Wang, S.S.-S.; Liu, K.-N.; Lee, W.-H. Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme. Biophys. Chem. 2009, 144, 78-87.
    • (2009) Biophys. Chem , vol.144 , pp. 78-87
    • Wang, S.S.1    Liu, K.-N.2    Lee, W.-H.3
  • 191
    • 84864944117 scopus 로고    scopus 로고
    • Curcumin’s pre-incubation temperature affects its inhibitory potency toward amyloid fibrillation and fibril-induced cytotoxicity of lysozyme
    • Liu, K.-N.; Lai, C.-M.; Lee, Y.-T.; Wang, S.-N.; Chen, R.P.-Y.; Jan, J.-S.; Liu, H.-S.; Wang, S.S.-S. Curcumin’s pre-incubation temperature affects its inhibitory potency toward amyloid fibrillation and fibril-induced cytotoxicity of lysozyme. Biochim. Biophys. Acta 2012, 1820, 1774-1786.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1774-1786
    • Liu, K.-N.1    Lai, C.-M.2    Lee, Y.-T.3    Wang, S.-N.4    Chen, R.P.5    Jan, J.-S.6    Liu, H.-S.7    Wang, S.S.8
  • 192
    • 84862275219 scopus 로고    scopus 로고
    • Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix
    • Sparks, S.; Liu, G.; Robbins, K.J.; Lazo, N.D. Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. Biochem. Biophys. Res. Commun. 2012, 422, 551-555.
    • (2012) Biochem. Biophys. Res. Commun , vol.422 , pp. 551-555
    • Sparks, S.1    Liu, G.2    Robbins, K.J.3    Lazo, N.D.4
  • 193
    • 78649301065 scopus 로고    scopus 로고
    • The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity
    • Daval, M.; Bedrood, S.; Gurlo, T.; Huang, C.J.; Costes, S.; Butler, P.C.; Langen, R. The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity. Amyloid 2010, 17, 118-128.
    • (2010) Amyloid , vol.17 , pp. 118-128
    • Daval, M.1    Bedrood, S.2    Gurlo, T.3    Huang, C.J.4    Costes, S.5    Butler, P.C.6    Langen, R.7
  • 195
    • 39849110292 scopus 로고    scopus 로고
    • Jerala, R. Curcumin binds to the α-helical intermediate and to the amyloid form of prion protein—A new mechanism for the inhibition of PrPSc accumulation
    • Bratkovič, I.H.; Gašperšič, J.; Šmid, L.M.; Bresjanac, M.; Jerala, R. Curcumin binds to the α-helical intermediate and to the amyloid form of prion protein—A new mechanism for the inhibition of PrPSc accumulation. J. Neurochem. 2008, 104, 1553-1564.
    • (2008) J. Neurochem , vol.104 , pp. 1553-1564
    • Bratkovič, I.H.1    Gašperšič, J.2    Šmid, L.M.3    Bresjanac, M.4
  • 197
    • 84858595914 scopus 로고    scopus 로고
    • Curcumin prevents aggregation in α-Synuclein by increasing reconfiguration rate
    • Ahmad, B.; Lapidus, L.J. Curcumin prevents aggregation in α-Synuclein by increasing reconfiguration rate. J. Biol. Chem. 2012, 287, 9193-9199.
    • (2012) J. Biol. Chem , vol.287 , pp. 9193-9199
    • Ahmad, B.1    Lapidus, L.J.2
  • 198
    • 84862498093 scopus 로고    scopus 로고
    • The effect of curcumin on the stability of Aβ dimers
    • Zhao, L.N.; Chiu, S.-W.; Benoit, J.; Chew, L.Y.; Mu, Y. The effect of curcumin on the stability of Aβ dimers. J. Phys. Chem. B. 2012, 116, 7428-7435.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7428-7435
    • Zhao, L.N.1    Chiu, S.-W.2    Benoit, J.3    Chew, L.Y.4    Mu, Y.5
  • 199
    • 33744918267 scopus 로고    scopus 로고
    • Molecular orbital basis for yellow curry spice curcumin’s prevention of Alzheimer’s disease
    • Balasubramanian, K. Molecular orbital basis for yellow curry spice curcumin’s prevention of Alzheimer’s disease. J. Agric. Food Chem. 2006, 54, 3512-3520.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 3512-3520
    • Balasubramanian, K.1
  • 201
    • 84858605051 scopus 로고    scopus 로고
    • A chemical analog of curcumin as an improved inhibitor of amyloid abeta oligomerization
    • Orlando, R.A.; Gonzales, A.M.; Royer, R.E.; Deck, L.M.; Vander Jagt, D.L. A chemical analog of curcumin as an improved inhibitor of amyloid abeta oligomerization. PLoS One 2012, 7, e31869.
    • (2012) Plos One , vol.7
    • Orlando, R.A.1    Gonzales, A.M.2    Royer, R.E.3    Deck, L.M.4    Vander Jagt, D.L.5
  • 202
    • 34548182307 scopus 로고    scopus 로고
    • Structure-activity relationships of amyloid beta-aggregation inhibitors based on curcumin: Influence of linker length and flexibility
    • Reinke, A.A.; Gestwickiusing, J.E. Structure-activity relationships of amyloid beta-aggregation inhibitors based on curcumin: Influence of linker length and flexibility. Chem. Biol. Drug Des. 2007, 70, 206-215.
    • (2007) Chem. Biol. Drug Des , vol.70 , pp. 206-215
    • Reinke, A.A.1    Gestwickiusing, J.E.2
  • 205
    • 84874114347 scopus 로고    scopus 로고
    • Curcumin and neurodegenerative diseases
    • Monroy, A.; Lithgow, G.J.; Alavez, S. Curcumin and neurodegenerative diseases. IUBMB Inc. 2013, 39, 122-132.
    • (2013) IUBMB Inc , vol.39 , pp. 122-132
    • Monroy, A.1    Lithgow, G.J.2    Alavez, S.3
  • 206
    • 0035930961 scopus 로고    scopus 로고
    • The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons
    • Choi, Y.T.; Jung, C.H.; Lee, S.R.; Bae, J.H.; Baek, W.K.; Suh, M.H.; Park, J.; Park, C.W.; Suh, S.I. The green tea polyphenol (-)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons. Life Sci. 2001, 70, 603-614.
    • (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    Park, J.7    Park, C.W.8    Suh, S.I.9
  • 207
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice
    • Rezai-Zadeh, K.; Shytle, D.; Sun, N.; Mori, T.; Hou, H.; Jeanniton, D.; Ehrhart, J.; Townsend, K.; Zeng, J.; Morgan, D. et al. Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J. Neurosci. 2005, 25, 8807-8814.
    • (2005) J. Neurosci , vol.25 , pp. 8807-8814
    • Rezai-Zadeh, K.1    Shytle, D.2    Sun, N.3    Mori, T.4    Hou, H.5    Jeanniton, D.6    Ehrhart, J.7    Townsend, K.8    Zeng, J.9    Morgan, D.10
  • 209
    • 33645294934 scopus 로고    scopus 로고
    • Reduction of iron-regulated amyloid precursor protein and beta-amyloid peptide by (-)-epigallocatechin-3-gallate in cell cultures: Implications for iron chelation in Alzheimer’s disease
    • Reznichenko, L.; Amit, T.; Zheng, H.; Avramovich-Tirosh, Y.; Youdim, M.B.; Weinreb, O.; Mandel, S. Reduction of iron-regulated amyloid precursor protein and beta-amyloid peptide by (-)-epigallocatechin-3-gallate in cell cultures: Implications for iron chelation in Alzheimer’s disease. J. Neurochem. 2006, 97, 527-536.
    • (2006) J. Neurochem , vol.97 , pp. 527-536
    • Reznichenko, L.1    Amit, T.2    Zheng, H.3    Avramovich-Tirosh, Y.4    Youdim, M.B.5    Weinreb, O.6    Mandel, S.7
  • 210
    • 33644949188 scopus 로고    scopus 로고
    • Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity
    • Bastianetto, S.; Yao, Z.X.; Papadopoulos, V.; Quirion, R. Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity. Eur. J. Neurosci. 2006, 23, 55-64.
    • (2006) Eur. J. Neurosci , vol.23 , pp. 55-64
    • Bastianetto, S.1    Yao, Z.X.2    Papadopoulos, V.3    Quirion, R.4
  • 214
    • 77956595088 scopus 로고    scopus 로고
    • The flavanol (−)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity
    • Meng, F.; Abedini, A.; Plesner, A.; Verchere, C.B.; Raleigh, D.P. The flavanol (−)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry 2010, 49, 8127-8133.
    • (2010) Biochemistry , vol.49 , pp. 8127-8133
    • Meng, F.1    Abedini, A.2    Plesner, A.3    Verchere, C.B.4    Raleigh, D.P.5
  • 215
    • 67049115575 scopus 로고    scopus 로고
    • The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection
    • Hauber, I.; Hohenberg, H.; Holstermann, B.; Hunstein, W.; Hauber, J. The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc. Natl. Acad. Sci. USA 2009, 106, 9033-9038.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5
  • 216
    • 72449188669 scopus 로고    scopus 로고
    • Tea catechins induce the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates
    • He, J.; Xing, Y.-F.; Huang, B.; Zhang, Y.-Z.; Zeng, C.-M. Tea catechins induce the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates. J. Agric. Food Chem. 2009, 57, 11391-11396.
    • (2009) J. Agric. Food Chem , vol.57 , pp. 11391-11396
    • He, J.1    Xing, Y.-F.2    Huang, B.3    Zhang, Y.-Z.4    Zeng, C.-M.5
  • 217
    • 69349098271 scopus 로고    scopus 로고
    • (−)-Epigallocatechin-3-Gallate (EGCG) maintains κ-casein in its pre-fibrillar state without redirecting its aggregation pathway
    • Hudson, S.A.; Ecroyd, H.; Dehle, F.C.; Musgrave, I.F.; Carver, J.A. (−)-Epigallocatechin-3-Gallate (EGCG) maintains κ-casein in its pre-fibrillar state without redirecting its aggregation pathway. J. Mol. Biol. 2009, 392, 689-700.
    • (2009) J. Mol. Biol , vol.392 , pp. 689-700
    • Hudson, S.A.1    Ecroyd, H.2    Dehle, F.C.3    Musgrave, I.F.4    Carver, J.A.5
  • 218
    • 84856492181 scopus 로고    scopus 로고
    • NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG
    • Huang, R.; Vivekanandan, S.; Brender, J.R.; Abe, Y.; Naito, A.; Ramamoorthy, A. NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG. J. Mol. Biol. 2012, 416, 108-120.
    • (2012) J. Mol. Biol , vol.416 , pp. 108-120
    • Huang, R.1    Vivekanandan, S.2    Brender, J.R.3    Abe, Y.4    Naito, A.5    Ramamoorthy, A.6
  • 220
    • 84859379008 scopus 로고    scopus 로고
    • Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols
    • Cao, P.; Raleigh, D.P. Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry 2012, 51, 2670-2683.
    • (2012) Biochemistry , vol.51 , pp. 2670-2683
    • Cao, P.1    Raleigh, D.P.2
  • 221
    • 84871664742 scopus 로고    scopus 로고
    • (-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme
    • Ghosh, S.; Pandey, N.K.; Dasgupta, S. (-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme. Int. J. Biol. Macromol. 2012, 54, 90-98.
    • (2012) Int. J. Biol. Macromol , vol.54 , pp. 90-98
    • Ghosh, S.1    Pandey, N.K.2    Dasgupta, S.3
  • 224
    • 84878234966 scopus 로고    scopus 로고
    • Toward the molecular mechanism(S) by which EGCG treatment remodels mature amyloid fibrils
    • Palhano, F.L.; Lee, J.; Grimster, N.P.; Kelly, J.W. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. J. Am Chem. Soc. 2013, 135, 7503-7510.
    • (2013) J. Am Chem. Soc , vol.135 , pp. 7503-7510
    • Palhano, F.L.1    Lee, J.2    Grimster, N.P.3    Kelly, J.W.4
  • 225
    • 77956307401 scopus 로고    scopus 로고
    • Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (−)-epigallocatechin-3-gallate
    • Wang, S.-H.; Liu, F.-F.; Dong, X.Y.; Sun Y. Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (−)-epigallocatechin-3-gallate. J. Phys. Chem. B 2010, 114, 11576-11583.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11576-11583
    • Wang, S.-H.1    Liu, F.-F.2    Dong, X.Y.3    Sun, Y.4
  • 226
    • 84862271632 scopus 로고    scopus 로고
    • Thermodynamic analysis of the molecular interactions between amyloid β-protein fragments and (−)-epigallocatechin-3-gallate
    • Wang, S.-H.; Dong, X.-Y.; Sun, Y. Thermodynamic analysis of the molecular interactions between amyloid β-protein fragments and (−)-epigallocatechin-3-gallate. J. Phys. Chem. B 2012, 116, 5803-5809.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5803-5809
    • Wang, S.-H.1    Dong, X.-Y.2    Sun, Y.3
  • 227
    • 84871570416 scopus 로고    scopus 로고
    • Inhibitory mechanism of pancreatic amyloid fibril formation: Formation of the complex between tea catechins and the fragment of residues 22-27
    • Kamihira-Ishijima, M.; Nakazawa, H.; Kira, A.; Naito, A.; Nakayama, T. Inhibitory mechanism of pancreatic amyloid fibril formation: Formation of the complex between tea catechins and the fragment of residues 22-27. Biochemistry 2012, 51, 10167-10174.
    • (2012) Biochemistry , vol.51 , pp. 10167-10174
    • Kamihira-Ishijima, M.1    Nakazawa, H.2    Kira, A.3    Naito, A.4    Nakayama, T.5
  • 228
    • 84866425464 scopus 로고    scopus 로고
    • The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution
    • Engel, M.F.M.; vandenAkker, C.C.; Schleeger, M.; Velikov, K.P.; Koenderink, G.H.; Bonn, M. The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution. J. Am. Chem. Soc. 2012, 134, 14781-14788.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 14781-14788
    • Engel, M.F.M.1    Vandenakker, C.C.2    Schleeger, M.3    Velikov, K.P.4    Koenderink, G.H.5    Bonn, M.6
  • 229
    • 79954762250 scopus 로고    scopus 로고
    • Interaction of epipcatechin gallate with phospholipid membranes as revealed by solid-state NMR spectroscopy. Biochim. Biophys
    • Uekusa, Y.; Kamihira-Lshijima, M.; Sugimoto, O.; Ishii, T.; Kumazawa, S.; Nakamura, K.; Tanji, K.; Naito, A.; Nakayama, T. Interaction of epipcatechin gallate with phospholipid membranes as revealed by solid-state NMR spectroscopy. Biochim. Biophys. Acta 2011, 1808, 1654-1660.
    • (2011) Acta , vol.1808 , pp. 1654-1660
    • Uekusa, Y.1    Kamihira-Lshijima, M.2    Sugimoto, O.3    Ishii, T.4    Kumazawa, S.5    Nakamura, K.6    Tanji, K.7    Naito, A.8    Nakayama, T.9
  • 230
    • 67749122326 scopus 로고    scopus 로고
    • Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: The case of the antioxidant curcumin
    • Barry, J.; Fritz, M.; Brender, J.R.; Smith, P.E.S.; Lee, D.K.; Ramamoorthy, A. Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: The case of the antioxidant curcumin. J. Am. Chem. Soc. 2009, 131, 4490-4498.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4490-4498
    • Barry, J.1    Fritz, M.2    Brender, J.R.3    Smith, P.E.S.4    Lee, D.K.5    Ramamoorthy, A.6
  • 232
    • 77954847105 scopus 로고    scopus 로고
    • The crystal structure of the green tea polyphenol (−)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site
    • Miyata, M.; Sato, T.; Kugimiya, M.; Sho, M.; Nakamura, T.; Ikemizu, S.; Chirifu, M.; Mizuguchi, M.; Nabeshima, Y.; Suwa, Y. et al. The crystal structure of the green tea polyphenol (−)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site. Biochemistry 2010, 49, 6104-6114.
    • (2010) Biochemistry , vol.49 , pp. 6104-6114
    • Miyata, M.1    Sato, T.2    Kugimiya, M.3    Sho, M.4    Nakamura, T.5    Ikemizu, S.6    Chirifu, M.7    Mizuguchi, M.8    Nabeshima, Y.9    Suwa, Y.10
  • 233
    • 0036801990 scopus 로고    scopus 로고
    • Pharmacokinetics of tea catechins after ingestion of green tea and (−)-epigallocatechin-3-gallate by humans: Formation of different metabolites and individual variability
    • Lee, M.J.; Maliakal, P.; Chen, L.; Meng, X.; Bondoc, F.Y.; Prabhu, S.; Lambert, G.; Mohr S.; Yang C.S. Pharmacokinetics of tea catechins after ingestion of green tea and (−)-epigallocatechin-3-gallate by humans: Formation of different metabolites and individual variability. Cancer Epidemiol. Biomark. Prev. 2002, 11, 1025-1032.
    • (2002) Cancer Epidemiol. Biomark. Prev , vol.11 , pp. 1025-1032
    • Lee, M.J.1    Maliakal, P.2    Chen, L.3    Meng, X.4    Bondoc, F.Y.5    Prabhu, S.6    Lambert, G.7    Mohr, S.8    Yang, C.S.9
  • 234
    • 80053207751 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate (EGCG) for clinical trials: More pitfalls than promises
    • Mereles, D.; Hunstein, W. Epigallocatechin-3-gallate (EGCG) for clinical trials: More pitfalls than promises? Int. J. Mol. Sci. 2011, 12, 5592-5603.
    • (2011) Int. J. Mol. Sci , vol.12 , pp. 5592-5603
    • Mereles, D.1    Hunstein, W.2
  • 235
    • 76749171209 scopus 로고    scopus 로고
    • Fish oil enhances anti-amyloidogenic properties of green tea EGCG in Tg2576 mice
    • Giunta, B.; Hou, H.; Zhu, Y.; Salemi, J.; Ruscin, A.; Shytle, R.D.; Tan, J. Fish oil enhances anti-amyloidogenic properties of green tea EGCG in Tg2576 mice. Neurosci. Lett. 2010, 471, 134-138.
    • (2010) Neurosci. Lett , vol.471 , pp. 134-138
    • Giunta, B.1    Hou, H.2    Zhu, Y.3    Salemi, J.4    Ruscin, A.5    Shytle, R.D.6    Tan, J.7
  • 236
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: The in vivo evidence
    • Baur, J.A.; Sinclair, D.A. Therapeutic potential of resveratrol: The in vivo evidence. Nat. Rev. Drug. Discov. 2006, 5, 493e506.
    • (2006) Nat. Rev. Drug. Discov , vol.5
    • Baur, J.A.1    Sinclair, D.A.2
  • 239
  • 240
    • 60249098801 scopus 로고    scopus 로고
    • Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer’s disease
    • Karuppagounder, S.S.; Pinto, J.T.; Xu, H.; Chen, H.-L.; Beal, M.F.; Gibson, G.E. Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer’s disease. Neurochem. Int. 2009, 54, 111-118.
    • (2009) Neurochem. Int , vol.54 , pp. 111-118
    • Karuppagounder, S.S.1    Pinto, J.T.2    Xu, H.3    Chen, H.-L.4    Beal, M.F.5    Gibson, G.E.6
  • 241
    • 84870239876 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of resveratrol derivatives as Aβ1-42 aggregation inhibitors, antioxidants, and neuroprotective agents
    • Lu, C.; Guo, Y.; Li, J.; Yao, M.; Liao, Q.; Xie, Z.; Li, X. Design, synthesis, and evaluation of resveratrol derivatives as Aβ1-42 aggregation inhibitors, antioxidants, and neuroprotective agents. Bioorg. Med. Chem. Lett. 2012, 22, 7683-7687.
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 7683-7687
    • Lu, C.1    Guo, Y.2    Li, J.3    Yao, M.4    Liao, Q.5    Xie, Z.6    Li, X.7
  • 243
    • 84858709095 scopus 로고    scopus 로고
    • Administration of resveratrol: What formulation solutions to bioavailability limitations
    • Amria, A.; Chaumeila, J.C.; Sfarb, S.; Charrueau, C. Administration of resveratrol: What formulation solutions to bioavailability limitations? J. Control Release 2012, 158, 182-193.
    • (2012) J. Control Release , vol.158 , pp. 182-193
    • Amria, A.1    Chaumeila, J.C.2    Sfarb, S.3    Charrueau, C.4
  • 244
    • 34249988863 scopus 로고    scopus 로고
    • Resveratrol oligomers from vitis amurensis attenuate β-amyloid-induced oxidative stress in PC12 cells
    • Jang, M.H.; Piao, X.L.; Kim, H.Y.; Cho, E.J.; Baek, S.H.; Kwon, S.W.; Park, H.L. Resveratrol oligomers from vitis amurensis attenuate β-amyloid-induced oxidative stress in PC12 cells. Biol. Pharm. Bull. 2007, 30, 1130-1134.
    • (2007) Biol. Pharm. Bull , vol.30 , pp. 1130-1134
    • Jang, M.H.1    Piao, X.L.2    Kim, H.Y.3    Cho, E.J.4    Baek, S.H.5    Kwon, S.W.6    Park, H.L.7
  • 245
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer’s disease amyloid-β peptides
    • Marambaud, P.; Zhao, H.; Davies, P. Resveratrol promotes clearance of Alzheimer’s disease amyloid-β peptides. J. Biol. Chem. 2005, 280, 37377-37382.
    • (2005) J. Biol. Chem , vol.280 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 246
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent β-amyloid toxicity through inhibiting NF-κB signaling
    • Chen, J.; Zhou, Y.; Mueller-Steiner, S.; Chen, L.F.; Kwon, H.; Yi, S.; Mucke, L.; Gan, L. SIRT1 protects against microglia-dependent β-amyloid toxicity through inhibiting NF-κB signaling. J. Biol. Chem. 2005, 280, 40364-40374.
    • (2005) J. Biol. Chem , vol.280 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6    Mucke, L.7    Gan, L.8
  • 247
    • 33644875954 scopus 로고    scopus 로고
    • Neuronal protection by sirtuins in Alzheimer’s disease
    • Anekonda, T.S.; Reddy, P.H. Neuronal protection by sirtuins in Alzheimer’s disease. J. Neurochem. 2006, 96, 305e13.
    • (2006) J. Neurochem , vol.96
    • Anekonda, T.S.1    Reddy, P.H.2
  • 249
    • 33745235570 scopus 로고    scopus 로고
    • Specific plasma membrane binding sites for polyphenols, including resveratrol, in the rat brain
    • Han, Y.S.; Bastianetto, S.; Dumont, Y.; Quirion, R. Specific plasma membrane binding sites for polyphenols, including resveratrol, in the rat brain. J. Pharmacol. Exp. Ther. 2006, 318, 238-245.
    • (2006) J. Pharmacol. Exp. Ther , vol.318 , pp. 238-245
    • Han, Y.S.1    Bastianetto, S.2    Dumont, Y.3    Quirion, R.4
  • 250
    • 60349096360 scopus 로고    scopus 로고
    • Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol
    • Mishra, R.; Sellin, D.; Radovan, D.; Gohlke, A.; Winter, R. Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol. Chembiochem 2009, 10, 445-449.
    • (2009) Chembiochem , vol.10 , pp. 445-449
    • Mishra, R.1    Sellin, D.2    Radovan, D.3    Gohlke, A.4    Winter, R.5
  • 251
    • 67650477387 scopus 로고    scopus 로고
    • Elucidating the mechanism of lipid membrane-induced IAPP fibrillogenesis and its inhibition by the red wine compound resveratrol: A synchrotron X-ray reflectivity study
    • Evers, F.; Jeworrek, C.; Tiemeyer, S.; Weise, K.; Sellin, D.; Paulus, M.; Struth, B.; Tolan, M.; Winter, R. Elucidating the mechanism of lipid membrane-induced IAPP fibrillogenesis and its inhibition by the red wine compound resveratrol: A synchrotron X-ray reflectivity study. J. Am. Chem. Soc. 2009, 131, 9516-9521.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9516-9521
    • Evers, F.1    Jeworrek, C.2    Tiemeyer, S.3    Weise, K.4    Sellin, D.5    Paulus, M.6    Struth, B.7    Tolan, M.8    Winter, R.9
  • 253
    • 67349252135 scopus 로고    scopus 로고
    • Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol
    • Radovan, D.; Opitz, N.; Winter, R. Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol. FEBS Lett. 2009, 583, 1439-1445.
    • (2009) FEBS Lett , vol.583 , pp. 1439-1445
    • Radovan, D.1    Opitz, N.2    Winter, R.3
  • 256
    • 84870057502 scopus 로고    scopus 로고
    • The binding of resveratrol to monomer and fibril amyloid beta
    • Ge, J.-F.; Qiao, J.-P.; Qi, C.-C.; Wang, C.-W.; Zhou, J.-N. The binding of resveratrol to monomer and fibril amyloid beta. Neurochem. Int. 2012, 61, 1192-1201.
    • (2012) Neurochem. Int , vol.61 , pp. 1192-1201
    • Ge, J.-F.1    Qiao, J.-P.2    Qi, C.-C.3    Wang, C.-W.4    Zhou, J.-N.5
  • 258
    • 84878141269 scopus 로고    scopus 로고
    • Amyloid aggregation of lysozyme: The synergy study of red wine polyphenols
    • Gazova, Z.; Siposova, K.; Kurin, E.; Mučaji, P.; Nagy, M. Amyloid aggregation of lysozyme: The synergy study of red wine polyphenols. Proteins 2013, doi:10.1002/prot.24250.
    • (2013) Proteins
    • Gazova, Z.1    Siposova, K.2    Kurin, E.3    Mučaji, P.4    Nagy, M.5
  • 259
    • 27744563958 scopus 로고    scopus 로고
    • Effects of naturally occurring compounds on fibril formation and oxidative stress of β-amyloid
    • Kim, H.; Park, B.-S.; Lee, K.-G.; Choi, C.Y.; Jang, S.S.; Kim, Y.-H.; Lee, S.-E. Effects of naturally occurring compounds on fibril formation and oxidative stress of β-amyloid. J. Agric. Food Chem. 2005, 53, 8537-8541.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8537-8541
    • Kim, H.1    Park, B.-S.2    Lee, K.-G.3    Choi, C.Y.4    Jang, S.S.5    Kim, Y.-H.6    Lee, S.-E.7
  • 261
    • 38849141961 scopus 로고    scopus 로고
    • Multifunction of myricetin on Aβ: Neuroprotection via a conformational change of Aβ and reduction of Aβ Via the interference of secretases
    • Shimmyo, Y.; Kihara, T.; Akaike, A.; Niidome, T.; Sugimoto, H. Multifunction of myricetin on Aβ: Neuroprotection via a conformational change of Aβ and reduction of Aβ Via the interference of secretases. J. Neurosci. Res. 2008, 86, 368-377.
    • (2008) J. Neurosci. Res , vol.86 , pp. 368-377
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 262
    • 84855895850 scopus 로고    scopus 로고
    • Quercetin inhibits amyloid fibrillation of bovine insulin and destabilizes preformed fibrils
    • Wang, J.B.; Wang, Y.M.; Zeng, C.M. Quercetin inhibits amyloid fibrillation of bovine insulin and destabilizes preformed fibrils. Biochem. Biophys. Res. Commun. 2011, 415, 675-679.
    • (2011) Biochem. Biophys. Res. Commun , vol.415 , pp. 675-679
    • Wang, J.B.1    Wang, Y.M.2    Zeng, C.M.3
  • 263
    • 33644945380 scopus 로고    scopus 로고
    • Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro
    • Ono, K.; Yamada, M. Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro. J. Neurochem. 2006, 97, 105-115.
    • (2006) J. Neurochem , vol.97 , pp. 105-115
    • Ono, K.1    Yamada, M.2
  • 264
    • 84856240878 scopus 로고    scopus 로고
    • Effect of phenolic compounds against Aβ aggregation and Aβ-induced toxicity in transgenic C. Elegans
    • Jagota, S.; Rajadas, J. Effect of phenolic compounds against Aβ aggregation and Aβ-induced toxicity in transgenic C. elegans. Neurochem. Res. 2012, 37, 40-48.
    • (2012) Neurochem. Res. , vol.37 , pp. 40-48
    • Jagota, S.1    Rajadas, J.2
  • 265
    • 84857403512 scopus 로고    scopus 로고
    • Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers
    • Noor, H.; Cao, P.; Raleigh, D.P. Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Sci. 2012, 21, 373-382.
    • (2012) Protein Sci , vol.21 , pp. 373-382
    • Noor, H.1    Cao, P.2    Raleigh, D.P.3
  • 266
    • 84863792805 scopus 로고    scopus 로고
    • Myricetin Inhibits islet amyloid polypeptide (IAPP) aggregation and rescues living mammalian cells from IAPP toxicity
    • Zelus, C.; Fox, A.; Calciano, A.; Faridian, B.S.; Nogaj, L.A.; Moffet, D.A. Myricetin Inhibits islet amyloid polypeptide (IAPP) aggregation and rescues living mammalian cells from IAPP toxicity. Open Biochem. J. 2012, 6, 66-70.
    • (2012) Open Biochem. J , vol.6 , pp. 66-70
    • Zelus, C.1    Fox, A.2    Calciano, A.3    Faridian, B.S.4    Nogaj, L.A.5    Moffet, D.A.6
  • 267
    • 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
  • 268
  • 269
    • 84869817141 scopus 로고    scopus 로고
    • Disclosure of a fundamental clue for the elucidation of the myricetin mechanism of action as amyloid aggregation inhibitor by mass spectrometry
    • Fiori, J.; Naldi, M.; Bartolini, M.; Andrisano, V. Disclosure of a fundamental clue for the elucidation of the myricetin mechanism of action as amyloid aggregation inhibitor by mass spectrometry. Electrophoresis 2012, 33, 3380-3386.
    • (2012) Electrophoresis , vol.33 , pp. 3380-3386
    • Fiori, J.1    Naldi, M.2    Bartolini, M.3    Andrisano, V.4
  • 270
    • 84860386735 scopus 로고    scopus 로고
    • Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding
    • Ono, K.; Li, L.; Takamura, Y.; Yoshiike, Y.; Zhu, L.; Han, F.; Mao, X.; Ikeda, T.; Takasaki, J.; Nishijo, H. et al. Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding. J. Biol. Chem. 2012, 287, 14631-14643.
    • (2012) J. Biol. Chem , vol.287 , pp. 14631-14643
    • Ono, K.1    Li, L.2    Takamura, Y.3    Yoshiike, Y.4    Zhu, L.5    Han, F.6    Mao, X.7    Ikeda, T.8    Takasaki, J.9    Nishijo, H.10
  • 271
    • 77952674128 scopus 로고    scopus 로고
    • Natural polyphenols as inhibitors of amyloid aggregation. Molecular dynamics study of GNNQQNY heptapeptide decamer
    • Berhanu, W.M.; Masunov, A.E. Natural polyphenols as inhibitors of amyloid aggregation. Molecular dynamics study of GNNQQNY heptapeptide decamer. Biophys. Chem. 2010, 149, 12-21.
    • (2010) Biophys. Chem , vol.149 , pp. 12-21
    • Berhanu, W.M.1    Masunov, A.E.2
  • 272
    • 79960740352 scopus 로고    scopus 로고
    • Resolution of localized small molecule-Aβ interactions by deep-ultraviolet resonance Raman spectroscopy
    • Wang, M.; Jiji, R.D. Resolution of localized small molecule-Aβ interactions by deep-ultraviolet resonance Raman spectroscopy. Biophys. Chem. 2011, 158, 96-103.
    • (2011) Biophys. Chem , vol.158 , pp. 96-103
    • Wang, M.1    Jiji, R.D.2
  • 273
    • 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. Biochi. Biophys. Acta 2008, 1780, 819-825.
    • (2008) Biochi. Biophys. Acta , vol.1780 , pp. 819-825
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 274
    • 61749103704 scopus 로고    scopus 로고
    • Protective effect of quercetin in primary neurons against Aβ(1-42): Relevance to Alzheimer’s disease
    • Ansari, M.A.; Abdul, H.M.; Joshi, G.; Opii, W.O.; Butterfield, D.A. Protective effect of quercetin in primary neurons against Aβ(1-42): Relevance to Alzheimer’s disease. J. Nutr. Biochem. 2009, 20, 269-275.
    • (2009) J. Nutr. Biochem , vol.20 , pp. 269-275
    • Ansari, M.A.1    Abdul, H.M.2    Joshi, G.3    Opii, W.O.4    Butterfield, D.A.5
  • 275
    • 67650690570 scopus 로고    scopus 로고
    • Protective effects of Ginkgo biloba extract (EGb761) and its constituents quercetin and ginkgolide B against β-amyloid peptide-induced toxicity in SH-SY5Y cells
    • Shi, C.; Zhao, L.; Zhu, B.; Li, Q.; Yew, D.T.; Yao, Z.; Xu, J. Protective effects of Ginkgo biloba extract (EGb761) and its constituents quercetin and ginkgolide B against β-amyloid peptide-induced toxicity in SH-SY5Y cells. Chem. Biol. Interact. 2009, 181, 115-123.
    • (2009) Chem. Biol. Interact , vol.181 , pp. 115-123
    • Shi, C.1    Zhao, L.2    Zhu, B.3    Li, Q.4    Yew, D.T.5    Yao, Z.6    Xu, J.7
  • 276
    • 79959922360 scopus 로고    scopus 로고
    • Nutritional approaches to modulate oxidative stress in Alzheimer’s disease
    • Pocernich, C.B.; Lange, M.L.; Sultana, R.; Butterfield, D.A. Nutritional approaches to modulate oxidative stress in Alzheimer’s disease. Curr. Alzheimer Res. 2011, 8, 452-469.
    • (2011) Curr. Alzheimer Res , vol.8 , pp. 452-469
    • Pocernich, C.B.1    Lange, M.L.2    Sultana, R.3    Butterfield, D.A.4
  • 277
    • 84872510192 scopus 로고    scopus 로고
    • Metal binding of flavonoids and their distinct inhibition mechanisms toward the oxidation activity of Cu2+-β-amyloid: Not just serving as suicide antioxidants!
    • Tay, W.M.; da Silva, G.F.Z.; Ming, L.-J. Metal binding of flavonoids and their distinct inhibition mechanisms toward the oxidation activity of Cu2+-β-amyloid: Not just serving as suicide antioxidants! Inorg. Chem. 2013, 52, 679-690.
    • (2013) Inorg. Chem , vol.52 , pp. 679-690
    • Tay, W.M.1    Da Silva, G.F.Z.2    Ming, L.-J.3
  • 278
    • 79955977168 scopus 로고    scopus 로고
    • Myricetin: A naturally occurring regulator of metal-induced amyloid-β aggregation and neurotoxicity
    • DeToma, A.S.; Choi, J.-S.; Braymer, J.J.; Lim, M.H. Myricetin: A naturally occurring regulator of metal-induced amyloid-β aggregation and neurotoxicity. Chembiochem 2011, 12, 1198-1201.
    • (2011) Chembiochem , vol.12 , pp. 1198-1201
    • Detoma, A.S.1    Choi, J.-S.2    Braymer, J.J.3    Lim, M.H.4
  • 279
    • 77957933189 scopus 로고    scopus 로고
    • Quercetin activates AMP-activated protein kinase by reducing PP2C expression protecting old mouse brain against high cholesterol-induced neurotoxicity
    • Lu, J.; Wu, D.M.; Zheng, Y.L.; Hu, B.; Zhang, Z.F.; Shan, Q.; Zheng, Z.H.; Liu, C.M.; Wang, Y.J. Quercetin activates AMP-activated protein kinase by reducing PP2C expression protecting old mouse brain against high cholesterol-induced neurotoxicity. J. Pathol. 2010, 222, 199-212.
    • (2010) J. Pathol , vol.222 , pp. 199-212
    • Lu, J.1    Wu, D.M.2    Zheng, Y.L.3    Hu, B.4    Zhang, Z.F.5    Shan, Q.6    Zheng, Z.H.7    Liu, C.M.8    Wang, Y.J.9
  • 280
    • 74949110261 scopus 로고    scopus 로고
    • Stimulation of neurogenesis and synaptogenesis by bilobalide and quercetin via common final pathway in hippocampal neurons
    • Tchantchou, F.; Lacor, P.N.; Cao, Z.; Lao, L.; Hou, Y.; Cui, C.; Klein, W.L.; Luo, Y. Stimulation of neurogenesis and synaptogenesis by bilobalide and quercetin via common final pathway in hippocampal neurons. J. Alzheimers Dis. 2009, 18, 787-798.
    • (2009) J. Alzheimers Dis , vol.18 , pp. 787-798
    • Tchantchou, F.1    Lacor, P.N.2    Cao, Z.3    Lao, L.4    Hou, Y.5    Cui, C.6    Klein, W.L.7    Luo, Y.8
  • 282
    • 45549099959 scopus 로고    scopus 로고
    • Three distinct neuroprotective functions of myricetin against glutamate-induced neuronal cell death: Involvement of direct inhibition of caspase-3
    • Shimmyo, Y.; Kihara, T.; Akaike, A.; Niidome, T.; Sugimoto, H. Three distinct neuroprotective functions of myricetin against glutamate-induced neuronal cell death: Involvement of direct inhibition of caspase-3. J. Neurosci. Res. 2008, 86, 1836-1845.
    • (2008) J. Neurosci. Res , vol.86 , pp. 1836-1845
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 283
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S.; Suzuki, N.; Masuda, M.; Hisanaga, S.; Iwatsubo, T.; Goedert, M.; Hasegawa, M. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 2005, 280, 7614-7623.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 289
    • 33646534602 scopus 로고    scopus 로고
    • Antioxidant effect of two virgin olive oils depends on the concentration and composition of minor polar compounds
    • Franconi, F.; Coinu, R.; Carta, S.; Urgeghe, P.P.; Ieri, F.; Mulinacci, N.; Romani, A. Antioxidant effect of two virgin olive oils depends on the concentration and composition of minor polar compounds. J. Agric. Food Chem. 2006, 54, 3121-3125.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 3121-3125
    • Franconi, F.1    Coinu, R.2    Carta, S.3    Urgeghe, P.P.4    Ieri, F.5    Mulinacci, N.6    Romani, A.7
  • 290
    • 20444476857 scopus 로고    scopus 로고
    • The phenolic compounds of olive oil: Structure, biological activity and beneficial effects on human health
    • Tripoli, E.; Giammanco, M.; Tabacchi, G.; Di Majo, D.; Giammanco, S.; La Guardia, M. The phenolic compounds of olive oil: Structure, biological activity and beneficial effects on human health. Nutr. Res. Rev. 2005, 18, 98-112.
    • (2005) Nutr. Res. Rev , vol.18 , pp. 98-112
    • Tripoli, E.1    Giammanco, M.2    Tabacchi, G.3    Di Majo, D.4    Giammanco, S.5    La Guardia, M.6
  • 292
    • 33645125772 scopus 로고    scopus 로고
    • Noncovalent interaction between amyloid-β-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry
    • Bazoti, F.N.; Berquist, J.; Markides, K.E.; Tsarbopoulos, A. Noncovalent interaction between amyloid-β-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 2006, 17, 568-575.
    • (2006) J. Am. Soc. Mass Spectrom , vol.17 , pp. 568-575
    • Bazoti, F.N.1    Berquist, J.2    Markides, K.E.3    Tsarbopoulos, A.4
  • 293
    • 48349093043 scopus 로고    scopus 로고
    • Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry
    • Bazoti, F.N.; Berquist, J.; Markides, K.E.; Tsarbopoulos, A. Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry. J. Am. Soc. Mass Spectrom. 2008, 19, 1078-1085.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1078-1085
    • Bazoti, F.N.1    Berquist, J.2    Markides, K.E.3    Tsarbopoulos, A.4
  • 297
    • 67649795090 scopus 로고    scopus 로고
    • Detection of interactions of the β-amyloid peptide with small molecules employing transferred NOEs
    • Benaki, D.; Stathopoulou, K.; Leondiadis, L.; Ferderigos, N.; Pelecanou, M.; Mikros, E. Detection of interactions of the β-amyloid peptide with small molecules employing transferred NOEs. J. Pept. Sci. 2009, 15, 435-441.
    • (2009) J. Pept. Sci , vol.15 , pp. 435-441
    • Benaki, D.1    Stathopoulou, K.2    Leondiadis, L.3    Ferderigos, N.4    Pelecanou, M.5    Mikros, E.6
  • 298
    • 80052906946 scopus 로고    scopus 로고
    • Study of the interaction between the amyloid beta peptide (1-40) and antioxidant compounds by nuclear magnetic resonance spectroscopy
    • Galanakis, P.A.; Bazoti, F.N.; Bergquist, J.; Markides, K.; Spyroulias, G.A.; Tsarbopoulos, A. Study of the interaction between the amyloid beta peptide (1-40) and antioxidant compounds by nuclear magnetic resonance spectroscopy. Biopolymers 2011, 96, 316-327.
    • (2011) Biopolymers , vol.96 , pp. 316-327
    • Galanakis, P.A.1    Bazoti, F.N.2    Bergquist, J.3    Markides, K.4    Spyroulias, G.A.5    Tsarbopoulos, A.6
  • 300
    • 82055197196 scopus 로고    scopus 로고
    • Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon
    • Rigacci, S.; Guidotti, V.; Bucciantini, M.; Nichino, D.; Relini, A.; Berti, A.; Stefani, M. Aβ(1-42) aggregates into non-toxic amyloid assemblies in the presence of the natural polyphenol oleuropein aglycon. Curr. Alzheimer Res. 2011, 8, 841-852.
    • (2011) Curr. Alzheimer Res , vol.8 , pp. 841-852
    • Rigacci, S.1    Guidotti, V.2    Bucciantini, M.3    Nichino, D.4    Relini, A.5    Berti, A.6    Stefani, M.7
  • 301
    • 84874778760 scopus 로고    scopus 로고
    • Oleuropein aglycone protects transgenic C. Elegans strains expressing Aβ42 by reducing plaque load and motor deficit
    • Diomede, L.; Rigacci, S.; Romeo, M.; Stefani, M.; Salmona, M. Oleuropein aglycone protects transgenic C. elegans strains expressing Aβ42 by reducing plaque load and motor deficit. PLoS One 2013, 8, e58893
    • (2013) Plos One , vol.8
    • Diomede, L.1    Rigacci, S.2    Romeo, M.3    Stefani, M.4    Salmona, M.5
  • 304
    • 84871820753 scopus 로고    scopus 로고
    • Oleuropein, an anti-oxidant polyphenol constituent of olive promotes α-secretase cleavage of the amyloid precursor protein (AβPP)
    • Kostomoiri, M.; Fragkouli, A.; Sagnou, M.; Skaltsounis, L.A.; Pelecanou, M.; Tsilibary, E.C.; Szinia, A.K. Oleuropein, an anti-oxidant polyphenol constituent of olive promotes α-secretase cleavage of the amyloid precursor protein (AβPP). Cell. Mol. Neurobiol. 2013, 33, 147-154.
    • (2013) Cell. Mol. Neurobiol , vol.33 , pp. 147-154
    • Kostomoiri, M.1    Fragkouli, A.2    Sagnou, M.3    Skaltsounis, L.A.4    Pelecanou, M.5    Tsilibary, E.C.6    Szinia, A.K.7
  • 306
    • 67651160771 scopus 로고    scopus 로고
    • Inhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau
    • Li, W.; Sperry, J.B.; Crowe, A.; Trojanowski, J.Q.; Smith, A.B; Lee, V.M.-Y. Inhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau. J. Neurochem. 2009, 110, 1339-1351.
    • (2009) J. Neurochem , vol.110 , pp. 1339-1351
    • Li, W.1    Sperry, J.B.2    Crowe, A.3    Trojanowski, J.Q.4    Smith, A.B.5    Lee, V.M.6
  • 307
    • 84867153806 scopus 로고    scopus 로고
    • Modulation of Tau protein fibrillization by Oleocanthal
    • Monti, M.C.; Margarucci, L.; Riccio, R.; Casapullo, A. Modulation of Tau protein fibrillization by Oleocanthal. J. Nat. Prod. 2012, 75, 1584-1588.
    • (2012) J. Nat. Prod , vol.75 , pp. 1584-1588
    • Monti, M.C.1    Margarucci, L.2    Riccio, R.3    Casapullo, A.4
  • 308
    • 84877120241 scopus 로고    scopus 로고
    • Olive-oil-derived oleocanthal enhances β-amyloid clearance as a potential neuroprotective mechanism against Alzheimer’s disease: In vitro and in vivo studies
    • Abuznait, A.H.; Qosa, H.; Busnena, B.A.; El Sayed, K.A.; Kaddoumi, A. Olive-oil-derived oleocanthal enhances β-amyloid clearance as a potential neuroprotective mechanism against Alzheimer’s disease: In vitro and in vivo studies. ACS Chem. Neurosci. 2013, doi:10.1021/cn400024q.
    • (2013) ACS Chem. Neurosci
    • Abuznait, A.H.1    Qosa, H.2    Busnena, B.A.3    El Sayed, K.A.4    Kaddoumi, A.5
  • 309
    • 84859198349 scopus 로고    scopus 로고
    • Distribution of olive oil phenolic compounds in rat tissues after administration of a phenolic extract from olive cake
    • Serra, A.; Rubio, L.; Borras, X.; Macia, A; Romero, M.P.; Motilva, M.J. Distribution of olive oil phenolic compounds in rat tissues after administration of a phenolic extract from olive cake. Mol. Nutr. Food Res. 2012, 3, 486-496.
    • (2012) Mol. Nutr. Food Res , vol.3 , pp. 486-496
    • Serra, A.1    Rubio, L.2    Borras, X.3    Macia, A.4    Romero, M.P.5    Motilva, M.J.6
  • 311
    • 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, 434-440.
    • (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
  • 312
    • 4944236514 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association
    • Moss, M.A.; Varvel, N.H.; Nichols, M.R.; Reed, D.K.; Rosenberry, T.L. Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association. Mol. Pharmacol. 2004, 66, 592-600.
    • (2004) Mol. Pharmacol , vol.66 , pp. 592-600
    • Moss, M.A.1    Varvel, N.H.2    Nichols, M.R.3    Reed, D.K.4    Rosenberry, T.L.5
  • 313
    • 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
  • 315
    • 82955223925 scopus 로고    scopus 로고
    • Identification of polyphenolic compounds and black tea extract as potent inhibitors of lipid membrane destabilization by Aβ42 aggregates
    • Gauci, A.J.; Caruana, M.; Giese, A.; Scerri, C.; Vassallo, N. Identification of polyphenolic compounds and black tea extract as potent inhibitors of lipid membrane destabilization by Aβ42 aggregates. J. Alzheimers Dis. 2011, 27, 767-779.
    • (2011) J. Alzheimers Dis. , vol.27 , pp. 767-779
    • Gauci, A.J.1    Caruana, M.2    Giese, A.3    Scerri, C.4    Vassallo, N.5
  • 316
    • 84871919725 scopus 로고    scopus 로고
    • Apigenin attenuates copper-mediated β-amyloid neurotoxicity through antioxidation, mitochondrion protection and MAPK signal inactivation in an AD cell model
    • Zhao, L.; Wang, J.L.; Wang, Y.R.; Fa, X.Z. Apigenin attenuates copper-mediated β-amyloid neurotoxicity through antioxidation, mitochondrion protection and MAPK signal inactivation in an AD cell model. Brain Res. 2013, 1492, 33-45.
    • (2013) Brain Res , vol.1492 , pp. 33-45
    • Zhao, L.1    Wang, J.L.2    Wang, Y.R.3    Fa, X.Z.4
  • 318
    • 79952010449 scopus 로고    scopus 로고
    • Baicalein inhibits formation of α-synuclein oligomers within living cells and prevents Aβ peptide fibrillation and oligomerisation
    • Lu, J.H.; Ardah, M.T.; Durairajan, S.S.; Liu, L.F.; Xie, L.X.; Fong, W.F.; Hasan, M.Y.; Huang, J.D.; El-Agnaf, O.M.; Li, M. Baicalein inhibits formation of α-synuclein oligomers within living cells and prevents Aβ peptide fibrillation and oligomerisation. Chembiochem 2011, 12, 615-624.
    • (2011) Chembiochem , vol.12 , pp. 615-624
    • Lu, J.H.1    Ardah, M.T.2    Durairajan, S.S.3    Liu, L.F.4    Xie, L.X.5    Fong, W.F.6    Hasan, M.Y.7    Huang, J.D.8    El-Agnaf, O.M.9    Li, M.10
  • 319
    • 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
  • 320
    • 77951912863 scopus 로고    scopus 로고
    • Destabilizing Alzheimer’s Abeta(42) protofibrils with morin: Mechanistic insights from molecular dynamics simulations
    • Lemkul, J.A.; Bevan, D.R. Destabilizing Alzheimer’s Abeta(42) protofibrils with morin: Mechanistic insights from molecular dynamics simulations. Biochemistry 2010, 49, 3935-3946.
    • (2010) Biochemistry , vol.49 , pp. 3935-3946
    • Lemkul, J.A.1    Bevan, D.R.2
  • 322
    • 84855730408 scopus 로고    scopus 로고
    • Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells
    • Jiménez-Aliaga, K.; Bermejo-Bescós, P.; Benedí, J.; Martín-Aragón, S. Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells. Life Sci. 2011, 89, 939-945.
    • (2011) Life Sci , vol.89 , pp. 939-945
    • Jiménez-Aliaga, K.1    Bermejo-Bescós, P.2    Benedí, J.3    Martín-Aragón, S.4
  • 323
    • 84861202049 scopus 로고    scopus 로고
    • Rutin inhibits β-amyloid aggregation and cytotoxicity, attenuates oxidative stress, and decreases the production of nitric oxide and proinflammatory cytokines
    • Wang, S.W.; Wang, Y.J.; Su, Y.J.; Zhou, W.W.; Yang, S.G.; Zhang, R.; Zhao, M.; Li, Y.N.; Zhang, Z.P.; Zhan, D.W. et al. Rutin inhibits β-amyloid aggregation and cytotoxicity, attenuates oxidative stress, and decreases the production of nitric oxide and proinflammatory cytokines. Neurotoxicology 2012, 33, 482-490.
    • (2012) Neurotoxicology , vol.33 , pp. 482-490
    • Wang, S.W.1    Wang, Y.J.2    Su, Y.J.3    Zhou, W.W.4    Yang, S.G.5    Zhang, R.6    Zhao, M.7    Li, Y.N.8    Zhang, Z.P.9    Zhan, D.W.10
  • 324
    • 79953095836 scopus 로고    scopus 로고
    • Luteolin isolated from the medicinal plant Elsholtzia rugulosa (Labiatae) prevents copper-mediated toxicity in β-amyloid precursor protein Swedish mutation overexpressing SH-SY5Y cells
    • Liu, R.; Meng, F.; Zhang, L.; Liu, A.; Qin, H.; Lan, X.; Li, L.; Du, G. Luteolin isolated from the medicinal plant Elsholtzia rugulosa (Labiatae) prevents copper-mediated toxicity in β-amyloid precursor protein Swedish mutation overexpressing SH-SY5Y cells. Molecules 2011, 16, 2084-2096.
    • (2011) Molecules , vol.16 , pp. 2084-2096
    • Liu, R.1    Meng, F.2    Zhang, L.3    Liu, A.4    Qin, H.5    Lan, X.6    Li, L.7    Du, G.8
  • 325
    • 79959977900 scopus 로고    scopus 로고
    • Rottlerin dissolves pre-formed protein amyloid: A study on hen egg white lysozyme
    • Sarkar, N.; Kumar, M.; Dubey, V.K. Rottlerin dissolves pre-formed protein amyloid: A study on hen egg white lysozyme. Biochim. Biophys. Acta 2011, 1810, 809-814.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 809-814
    • Sarkar, N.1    Kumar, M.2    Dubey, V.K.3
  • 328
    • 60349116815 scopus 로고    scopus 로고
    • Comparative neuroprotective properties of stilbene and catechin analogs: Action via a plasma membrane receptor site?
    • Bastianetto, S.; Dumont, Y.; Han, Y.; Quirion, R. Comparative neuroprotective properties of stilbene and catechin analogs: Action via a plasma membrane receptor site? CNS Neurosci. Ther. 2009, 15, 76-83.
    • (2009) CNS Neurosci. Ther , vol.15 , pp. 76-83
    • Bastianetto, S.1    Dumont, Y.2    Han, Y.3    Quirion, R.4
  • 330
    • 24644438783 scopus 로고    scopus 로고
    • Ferulic acid destabilizes preformed beta-amyloid fibrils in vitro
    • Ono, K.; Hirohata, M.; Yamada, M. Ferulic acid destabilizes preformed beta-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
  • 331
    • 84873723882 scopus 로고    scopus 로고
    • The effects of ferulic acid on β-amyloid fibrillar structures investigated through experimental and computational techniques
    • Sgarbossa, A.; Monti, S.; Lenci, F.; Bramanti, E.; Bizzarri, R.; Barone, V. The effects of ferulic acid on β-amyloid fibrillar structures investigated through experimental and computational techniques. Biochim. Biophys. Acta 2013, 1830, 2924-2937.
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 2924-2937
    • Sgarbossa, A.1    Monti, S.2    Lenci, F.3    Bramanti, E.4    Bizzarri, R.5    Barone, V.6
  • 332
    • 84872720134 scopus 로고    scopus 로고
    • Protective effects of ferulic acid in amyloid precursor protein plus presenilin-1 transgenic mouse model of Alzheimer disease
    • Yan, J.J.; Jung, J.S.; Kim, T.K.; Hasan, A.; Hong, C.W.; Nam, J.S.; Song, D.K. Protective effects of ferulic acid in amyloid precursor protein plus presenilin-1 transgenic mouse model of Alzheimer disease. Biol. Pharm. Bull. 2013, 36, 140-143.
    • (2013) Biol. Pharm. Bull , vol.36 , pp. 140-143
    • Yan, J.J.1    Jung, J.S.2    Kim, T.K.3    Hasan, A.4    Hong, C.W.5    Nam, J.S.6    Song, D.K.7


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