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Volumn 51, Issue 2, 2015, Pages 466-479

Polyphenols as Therapeutic Molecules in Alzheimer’s Disease Through Modulating Amyloid Pathways

Author keywords

Alzheimer s disease; Amyloid fibril disaggregation; A aggregation; Molecular mechanisms; Polyphenols; Structure activity relationships; Secretase activator; Secretase inhibitor; Secretase inhibitor

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; POLYPHENOL;

EID: 84939877810     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-014-8722-9     Document Type: Review
Times cited : (100)

References (146)
  • 1
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer’s and Parkinson’s diseases. Neuromolecular Med 4:21–36
    • Hashimoto M, Rockenstein E, Crews L, Masliah E (2003) Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer’s and Parkinson’s diseases. Neuromolecular Med 4:21–36. doi:10.1385/NMM:4:1-2:21
    • (2003) doi:10.1385/NMM:4:1-2:21
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 2
    • 79952706244 scopus 로고    scopus 로고
    • Exploring the inhibitory activity of short-chain phospholipids against amyloid fibrillogenesis of hen egg-white lysozyme
    • COI: 1:CAS:528:DC%2BC3MXksFKlsr4%3D, PID: 21320633
    • Wang SS, Hung YT, Wen WS, Lin KC, Chen GY (2011) Exploring the inhibitory activity of short-chain phospholipids against amyloid fibrillogenesis of hen egg-white lysozyme. Biochim Biophys Acta 1811:301–313. doi:10.1016/j.bbalip.2011.02.003
    • (2011) Biochim Biophys Acta , vol.1811 , pp. 301-313
    • Wang, S.S.1    Hung, Y.T.2    Wen, W.S.3    Lin, K.C.4    Chen, G.Y.5
  • 3
    • 79955671043 scopus 로고    scopus 로고
    • Targeting oligomers in neurodegenerative disorders: lessons from α-synuclein, tau, and amyloid-β peptide
    • COI: 1:CAS:528:DC%2BC3MXltFGrt74%3D, PID: 21460436
    • Gadad BS, Britton GB, Rao KS (2011) Targeting oligomers in neurodegenerative disorders: lessons from α-synuclein, tau, and amyloid-β peptide. J Alzheimers Dis 24:223–232. doi:10.3233/JAD-2011-110182
    • (2011) J Alzheimers Dis , vol.24 , pp. 223-232
    • Gadad, B.S.1    Britton, G.B.2    Rao, K.S.3
  • 4
    • 79955671212 scopus 로고    scopus 로고
    • Oxidative genome damage and its repair in neurodegenerative diseases: function of transition metals as a double-edged sword
    • COI: 1:CAS:528:DC%2BC3MXltFGrt7o%3D, PID: 21441656
    • Hegde ML, Hegde PM, Rao KS, Mitra S (2011) Oxidative genome damage and its repair in neurodegenerative diseases: function of transition metals as a double-edged sword. J Alzheimers Dis 24:183–198. doi:10.3233/JAD-2011-110281
    • (2011) J Alzheimers Dis , vol.24 , pp. 183-198
    • Hegde, M.L.1    Hegde, P.M.2    Rao, K.S.3    Mitra, S.4
  • 5
    • 84885468645 scopus 로고    scopus 로고
    • Recent advances in α-synuclein functions, advanced glycation, and toxicity: implications for Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3sXjsFejs70%3D, PID: 22923367
    • Guerrero E, Padmaraju V, Hegde ML, Britton GB, Rao KS (2013) Recent advances in α-synuclein functions, advanced glycation, and toxicity: implications for Parkinson’s disease. Mol Neurobiol 47:525–536
    • (2013) Mol Neurobiol , vol.47 , pp. 525-536
    • Guerrero, E.1    Padmaraju, V.2    Hegde, M.L.3    Britton, G.B.4    Rao, K.S.5
  • 6
    • 84861153988 scopus 로고    scopus 로고
    • Review of theoretical studies for prediction of neurodegenerative inhibitors
    • COI: 1:CAS:528:DC%2BC38XoslCktb8%3D, PID: 22587762
    • Prado-Prado F, García I (2012) Review of theoretical studies for prediction of neurodegenerative inhibitors. Mini Rev Med Chem 12:452–466. doi:10.2174/138955712800493780
    • (2012) Mini Rev Med Chem , vol.12 , pp. 452-466
    • Prado-Prado, F.1    García, I.2
  • 7
    • 84862786944 scopus 로고    scopus 로고
    • Cholinestrase inhibitory effects of geranylated flavonoids from Paulownia tomentosa fruits
    • COI: 1:CAS:528:DC%2BC38XkvFSqs7c%3D, PID: 22445674
    • Cho JK, Ryu YB, Curtis-Long MJ, Ryu HW, Yuk HJ, Kim DW, Kim HJ, Lee WS, Park KH (2012) Cholinestrase inhibitory effects of geranylated flavonoids from Paulownia tomentosa fruits. Bioorg Med Chem 20:2595–2602. doi:10.1016/j.bmc.2012.02.044
    • (2012) Bioorg Med Chem , vol.20 , pp. 2595-2602
    • Cho, J.K.1    Ryu, Y.B.2    Curtis-Long, M.J.3    Ryu, H.W.4    Yuk, H.J.5    Kim, D.W.6    Kim, H.J.7    Lee, W.S.8    Park, K.H.9
  • 9
    • 33748742887 scopus 로고    scopus 로고
    • Neurine, an acetylcholine autolysis product, elevates secreted amyloid-β protein precursor and amyloid-β peptide levels, and lowers neuronal cell viability in culture: a role in Alzheimer’s disease?
    • COI: 1:CAS:528:DC%2BD28XpsValt74%3D, PID: 16988475
    • Tweedie D, Brossi A, Chen D, Ge YW, Bailey J, Yu QS, Kamal MA, Sambamurti K, Lahiri DK, Greig NH (2006) Neurine, an acetylcholine autolysis product, elevates secreted amyloid-β protein precursor and amyloid-β peptide levels, and lowers neuronal cell viability in culture: a role in Alzheimer’s disease? J Alzheimers Dis 10:9–16
    • (2006) J Alzheimers Dis , vol.10 , pp. 9-16
    • Tweedie, D.1    Brossi, A.2    Chen, D.3    Ge, Y.W.4    Bailey, J.5    Yu, Q.S.6    Kamal, M.A.7    Sambamurti, K.8    Lahiri, D.K.9    Greig, N.H.10
  • 10
    • 77950362845 scopus 로고    scopus 로고
    • Neuronutrition and Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC3cXjslamsbY%3D, PID: 20308778
    • Ramesh BN, Rao TSS, Prakasam A, Sambamurti K, Rao KS (2010) Neuronutrition and Alzheimer’s disease. J Alzheimers Dis 19:1123–1139. doi:10.3233/JAD-2010-1312
    • (2010) J Alzheimers Dis , vol.19 , pp. 1123-1139
    • Ramesh, B.N.1    Rao, T.S.S.2    Prakasam, A.3    Sambamurti, K.4    Rao, K.S.5
  • 12
    • 77953544705 scopus 로고    scopus 로고
    • New evidences on Tau–DNA interactions and relevance to neurodegeneration
    • COI: 1:CAS:528:DC%2BC3cXntVeltrs%3D, PID: 20435075
    • Padmaraju V, Indi SS, Rao KS (2010) New evidences on Tau–DNA interactions and relevance to neurodegeneration. Neurochem Int 57:51–57. doi:10.1016/j.neuint.2010.04.013
    • (2010) Neurochem Int , vol.57 , pp. 51-57
    • Padmaraju, V.1    Indi, S.S.2    Rao, K.S.3
  • 13
    • 38549142362 scopus 로고    scopus 로고
    • Amyloid and tau imaging, neuronal losses and function in mild cognitive impairment
    • COI: 1:STN:280:DC%2BD1c%2Fgt1GitA%3D%3D, PID: 18165848
    • Barrio JR, Kepe V, Satyamurthy N, Huang SC, Small G (2008) Amyloid and tau imaging, neuronal losses and function in mild cognitive impairment. J Nutr Health Aging 12:61S–65S
    • (2008) J Nutr Health Aging , vol.12 , pp. 61S-65S
    • Barrio, J.R.1    Kepe, V.2    Satyamurthy, N.3    Huang, S.C.4    Small, G.5
  • 14
    • 47849093351 scopus 로고    scopus 로고
    • Value in development of a TAPIR-like mouse monoclonal antibody to Aβ
    • PID: 18663823
    • Sambamurti K, Pappolla MA, Rao KS (2008) Value in development of a TAPIR-like mouse monoclonal antibody to Aβ. J Alzheimers Dis 14:175–177
    • (2008) J Alzheimers Dis , vol.14 , pp. 175-177
    • Sambamurti, K.1    Pappolla, M.A.2    Rao, K.S.3
  • 15
    • 33745966453 scopus 로고    scopus 로고
    • Identification of novel small molecule inhibitors of amyloid precursor protein synthesis as a route to lower Alzheimer’s disease amyloid-β peptide
    • COI: 1:CAS:528:DC%2BD28XnslOlt7o%3D, PID: 16690718
    • Utsuki T, Yu QS, Davidson D, Chen D, Holloway HW, Brossi A, Sambamurti K, Lahiri DK, Greig NH, Giordano T (2006) Identification of novel small molecule inhibitors of amyloid precursor protein synthesis as a route to lower Alzheimer’s disease amyloid-β peptide. J Pharmacol Exp Ther 318:855–862. doi:10.1124/jpet.106.103309
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 855-862
    • Utsuki, T.1    Yu, Q.S.2    Davidson, D.3    Chen, D.4    Holloway, H.W.5    Brossi, A.6    Sambamurti, K.7    Lahiri, D.K.8    Greig, N.H.9    Giordano, T.10
  • 16
    • 3242682709 scopus 로고    scopus 로고
    • Deposition of amyloid fibrils promotes cell-surface accumulation of amyloid β precursor protein
    • COI: 1:CAS:528:DC%2BD2cXlslyjsrw%3D, PID: 15262274
    • Heredia L, Lin R, Vigo FS, Kedikian G, Busciglio J, Lorenzo A (2004) Deposition of amyloid fibrils promotes cell-surface accumulation of amyloid β precursor protein. Neurobiol Dis 16:617–629. doi:10.1016/j.nbd.2004.04.015
    • (2004) Neurobiol Dis , vol.16 , pp. 617-629
    • Heredia, L.1    Lin, R.2    Vigo, F.S.3    Kedikian, G.4    Busciglio, J.5    Lorenzo, A.6
  • 17
    • 84891871121 scopus 로고    scopus 로고
    • Emerging therapeutics for Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC2cXjsVSqt7s%3D, PID: 24392696
    • Chiang K, Koo E (2014) Emerging therapeutics for Alzheimer’s disease. Annu Rev Pharmacol Toxicol 54:381–405
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 381-405
    • Chiang, K.1    Koo, E.2
  • 18
    • 84877064788 scopus 로고    scopus 로고
    • Clinical trials in predementia stages of Alzheimer disease
    • PID: 23642580
    • Pillai JA, Cummings JL (2013) Clinical trials in predementia stages of Alzheimer disease. Med Clin North Am 97:439–457. doi:10.1016/j.mcna.2013.01.002
    • (2013) Med Clin North Am , vol.97 , pp. 439-457
    • Pillai, J.A.1    Cummings, J.L.2
  • 19
    • 84879283895 scopus 로고    scopus 로고
    • Treatment strategies targeting amyloid β-protein
    • PID: 22951439
    • Schenk D, Basi GS, Pangalos MN (2012) Treatment strategies targeting amyloid β-protein. Cold Spring Harb Perspect Med 2:a006387. doi:10.1101/cshperspect.a006387
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006387
    • Schenk, D.1    Basi, G.S.2    Pangalos, M.N.3
  • 20
    • 67649544381 scopus 로고    scopus 로고
    • Biomarker discovery in neurodegenerative diseases: a proteomic approach
    • COI: 1:CAS:528:DC%2BD1MXotFCgtrk%3D, PID: 18938247
    • Shi M, Caudle WM, Zhang J (2009) Biomarker discovery in neurodegenerative diseases: a proteomic approach. Neurobiol Dis 35:157–164. doi:10.1016/j.nbd.2008.09.004
    • (2009) Neurobiol Dis , vol.35 , pp. 157-164
    • Shi, M.1    Caudle, W.M.2    Zhang, J.3
  • 21
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics
    • COI: 1:CAS:528:DC%2BD38Xls1Cju7s%3D, PID: 12130773
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297:353–356. doi:10.1126/science.1072994
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 22
    • 33750885775 scopus 로고    scopus 로고
    • Molecular and biochemical features in Alzheimer’s disease
    • PID: 17105434
    • Pallàs M, Camins A (2006) Molecular and biochemical features in Alzheimer’s disease. Curr Pharm Des 12:4389–4408
    • (2006) Curr Pharm Des , vol.12 , pp. 4389-4408
    • Pallàs, M.1    Camins, A.2
  • 23
    • 84866668465 scopus 로고    scopus 로고
    • Neuroprotective potential of phytochemicals
    • PID: 23055633
    • Kumar GP, Khanum F (2012) Neuroprotective potential of phytochemicals. Pharmacogn Rev 6:81–90. doi:10.4103/0973-7847.99898
    • (2012) Pharmacogn Rev , vol.6 , pp. 81-90
    • Kumar, G.P.1    Khanum, F.2
  • 24
    • 84893908949 scopus 로고    scopus 로고
    • In vitro evidence that an aqueous extract of Centella asiatica modulates α-synuclein aggregation dynamics
    • PID: 24284367
    • Berrocal R, Vasudevaraju P, Indi SS, Sambasiva Rao KR, Rao KS (2014) In vitro evidence that an aqueous extract of Centella asiatica modulates α-synuclein aggregation dynamics. J Alzheimers Dis 39(2):457–465. doi:10.3233/JAD-131187
    • (2014) J Alzheimers Dis , vol.39 , Issue.2 , pp. 457-465
    • Berrocal, R.1    Vasudevaraju, P.2    Indi, S.S.3    Sambasiva Rao, K.R.4    Rao, K.S.5
  • 25
    • 77952885334 scopus 로고    scopus 로고
    • Anti-amyloidogenic property of leaf aqueous extract of Caesalpinia crista
    • COI: 1:CAS:528:DC%2BC3cXltFOmsLY%3D, PID: 20356566
    • Ramesh BN, Indi SS, Rao KS (2010) Anti-amyloidogenic property of leaf aqueous extract of Caesalpinia crista. Neurosci Lett 475:110–114. doi:10.1016/j.neulet.2010.03.062
    • (2010) Neurosci Lett , vol.475 , pp. 110-114
    • Ramesh, B.N.1    Indi, S.S.2    Rao, K.S.3
  • 26
    • 78449248935 scopus 로고    scopus 로고
    • Potential therapeutic agents against Alzheimer’s disease from natural sources
    • COI: 1:CAS:528:DC%2BC3cXhtlOqtr%2FN, PID: 21052936
    • Park SY (2010) Potential therapeutic agents against Alzheimer’s disease from natural sources. Arch Pharm Res 33:1589–1609. doi:10.1007/s12272-010-1010-y
    • (2010) Arch Pharm Res , vol.33 , pp. 1589-1609
    • Park, S.Y.1
  • 28
    • 77951281689 scopus 로고    scopus 로고
    • Systematic analysis of the content of 502 polyphenols in 452 foods and beverages: an application of the phenol-explorer database
    • PID: 20302342
    • Pérez-Jiménez J, Neveu V, Vos F, Scalbert A (2010) Systematic analysis of the content of 502 polyphenols in 452 foods and beverages: an application of the phenol-explorer database. J Agric Food Chem 58:4959–4969. doi:10.1021/jf100128b
    • (2010) J Agric Food Chem , vol.58 , pp. 4959-4969
    • Pérez-Jiménez, J.1    Neveu, V.2    Vos, F.3    Scalbert, A.4
  • 29
    • 0034736046 scopus 로고    scopus 로고
    • Advances in flavonoid research since 1992
    • COI: 1:CAS:528:DC%2BD3cXosFent74%3D, PID: 11130659
    • Harborne JB, Williams CA (2000) Advances in flavonoid research since 1992. Phytochemistry 55:481–504
    • (2000) Phytochemistry , vol.55 , pp. 481-504
    • Harborne, J.B.1    Williams, C.A.2
  • 30
    • 79551573834 scopus 로고    scopus 로고
    • A critical review of methods for characterisation of polyphenolic compounds in fruits and vegetables
    • COI: 1:CAS:528:DC%2BC3MXht1Wlt7Y%3D, PID: 25213963
    • Ignat I, Volf I, Popa VI (2011) A critical review of methods for characterisation of polyphenolic compounds in fruits and vegetables. Food Chem 126:1821–1835. doi:10.1016/j.foodchem.2010.12.026
    • (2011) Food Chem , vol.126 , pp. 1821-1835
    • Ignat, I.1    Volf, I.2    Popa, V.I.3
  • 31
    • 79960841853 scopus 로고    scopus 로고
    • Polyphenol contents and radical scavenging capacities of red maple (Acer rubrum L.) extracts
    • COI: 1:CAS:528:DC%2BC3MXps12hsL4%3D, PID: 21683113
    • Royer M, Diouf PN, Stevanovic T (2011) Polyphenol contents and radical scavenging capacities of red maple (Acer rubrum L.) extracts. Food Chem Toxicol 49:2180–2188. doi:10.1016/j.fct.2011.06.003
    • (2011) Food Chem Toxicol , vol.49 , pp. 2180-2188
    • Royer, M.1    Diouf, P.N.2    Stevanovic, T.3
  • 32
    • 33645451444 scopus 로고    scopus 로고
    • Effects of anthocyanins and other phenolics of boysenberry and blackcurrant as inhibitors of oxidative stress and damage to cellular DNA in SH-SY5Y and HL-60 cells
    • COI: 1:CAS:528:DC%2BD28XjtlKlsrs%3D
    • Ghosh D, McGhie TK, Zhang J, Adaim A, Skinner M (2006) Effects of anthocyanins and other phenolics of boysenberry and blackcurrant as inhibitors of oxidative stress and damage to cellular DNA in SH-SY5Y and HL-60 cells. J Sci Food Agric 86:678–686. doi:10.1002/jsfa.2409
    • (2006) J Sci Food Agric , vol.86 , pp. 678-686
    • Ghosh, D.1    McGhie, T.K.2    Zhang, J.3    Adaim, A.4    Skinner, M.5
  • 33
    • 80051842687 scopus 로고    scopus 로고
    • 2-induced cytotoxicity in PC12 cells
    • COI: 1:CAS:528:DC%2BD1cXlsl2quw%3D%3D, PID: 18189359
    • 2-induced cytotoxicity in PC12 cells. J Agric Food Chem 56:859–864. doi:10.1021/jf072826r
    • (2008) J Agric Food Chem , vol.56 , pp. 859-864
    • Hwang, S.L.1    Yen, G.C.2
  • 34
    • 1642266586 scopus 로고    scopus 로고
    • Effect of antioxidant flavanone, naringenin, from Citrus junos on neuroprotection
    • COI: 1:CAS:528:DC%2BD2cXhsFyhsLY%3D, PID: 15030205
    • Heo HJ, Kim DO, Shin SC, Kim MJ, Kim BG, Shin DH (2004) Effect of antioxidant flavanone, naringenin, from Citrus junos on neuroprotection. J Agric Food Chem 52:1520–1525. doi:10.1021/jf035079g
    • (2004) J Agric Food Chem , vol.52 , pp. 1520-1525
    • Heo, H.J.1    Kim, D.O.2    Shin, S.C.3    Kim, M.J.4    Kim, B.G.5    Shin, D.H.6
  • 35
    • 84870210315 scopus 로고    scopus 로고
    • Antioxidant activity and polyphenol content in cultivated and wild edible fruits grown in Panama
    • Murillo E, Britton GB, Durant AA (2012) Antioxidant activity and polyphenol content in cultivated and wild edible fruits grown in Panama. J Pharm Bioall Sci 4:313–317. doi:10.4103/0975-7406.103261
    • (2012) J Pharm Bioall Sci , vol.4 , pp. 313-317
    • Murillo, E.1    Britton, G.B.2    Durant, A.A.3
  • 37
    • 34147136736 scopus 로고    scopus 로고
    • Effect of the citrus flavanone naringenin on oxidative stress in rats
    • COI: 1:CAS:528:DC%2BD2sXhvFagsrc%3D, PID: 17315884
    • Andrade JE, Burgess JR (2007) Effect of the citrus flavanone naringenin on oxidative stress in rats. J Agric Food Chem 55:2142–2148. doi:10.1021/jf061714h
    • (2007) J Agric Food Chem , vol.55 , pp. 2142-2148
    • Andrade, J.E.1    Burgess, J.R.2
  • 38
    • 21544443151 scopus 로고    scopus 로고
    • Contents of polyphenols in fruit and vegetables
    • Cieślik E, Gręda A, Adamus W (2006) Contents of polyphenols in fruit and vegetables. Food Chem 94:135–142. doi:10.1016/j.foodchem.2004.11.015
    • (2006) Food Chem , vol.94 , pp. 135-142
    • Cieślik, E.1    Gręda, A.2    Adamus, W.3
  • 39
    • 70350645117 scopus 로고    scopus 로고
    • Identification and characterization of polyphenolic antioxidants using on-line liquid chromatography, electrochemistry, and electrospray ionization tandem mass spectrometry
    • COI: 1:CAS:528:DC%2BD1MXhtFyqsrrJ, PID: 19785449
    • Zettersten C, Co M, Wende S, Turner C, Nyholm L, Sjöberg PJR (2009) Identification and characterization of polyphenolic antioxidants using on-line liquid chromatography, electrochemistry, and electrospray ionization tandem mass spectrometry. Anal Chem 81:8968–8977. doi:10.1021/ac901397c
    • (2009) Anal Chem , vol.81 , pp. 8968-8977
    • Zettersten, C.1    Co, M.2    Wende, S.3    Turner, C.4    Nyholm, L.5    Sjöberg, P.J.R.6
  • 40
    • 0141673338 scopus 로고    scopus 로고
    • Optimization of a new mobile phase to know the complex and real polyphenolic composition: towards a total phenolic index using high-performance liquid chromatography
    • COI: 1:CAS:528:DC%2BD3sXnvFWjtbg%3D, PID: 14582624
    • Tsao R, Yang R (2003) Optimization of a new mobile phase to know the complex and real polyphenolic composition: towards a total phenolic index using high-performance liquid chromatography. J Chromatogr A 1018:29–40. doi:10.1016/j.chroma.2003.08.034
    • (2003) J Chromatogr A , vol.1018 , pp. 29-40
    • Tsao, R.1    Yang, R.2
  • 41
    • 0031721802 scopus 로고    scopus 로고
    • Polyphenols: chemistry, dietary sources, metabolism, and nutritional significance
    • COI: 1:STN:280:DyaK1M%2Fls1WktQ%3D%3D, PID: 9838798
    • Bravo L (1998) Polyphenols: chemistry, dietary sources, metabolism, and nutritional significance. Nutr Rev 56:317–333
    • (1998) Nutr Rev , vol.56 , pp. 317-333
    • Bravo, L.1
  • 42
    • 47849120398 scopus 로고    scopus 로고
    • Challenges for research on polyphenols from foods in Alzheimer’s disease: bioavailability, metabolism, and cellular and molecular mechanisms
    • COI: 1:CAS:528:DC%2BD1cXnt1Wis7w%3D, PID: 18557624
    • Singh MA, Arseneault MA, Sanderson T, Murthy VEN, Ramassamy C (2008) Challenges for research on polyphenols from foods in Alzheimer’s disease: bioavailability, metabolism, and cellular and molecular mechanisms. J Agric Food Chem 56:4855–4873
    • (2008) J Agric Food Chem , vol.56 , pp. 4855-4873
    • Singh, M.A.1    Arseneault, M.A.2    Sanderson, T.3    Murthy, V.E.N.4    Ramassamy, C.5
  • 44
    • 0037117475 scopus 로고    scopus 로고
    • Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity
    • COI: 1:CAS:528:DC%2BD38XjtFKls7w%3D, PID: 11959984
    • Jez JM, Bowman ME, Noel JP (2002) Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity. Proc Natl Acad Sci 99:5319–5324. doi:10.1073/pnas.082590499
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 5319-5324
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 45
    • 33747115357 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids, polyunsaturated fatty acids and flavonoids in Saccharomyces cerevisiae
    • PID: 16719921
    • Chemler JA, Yan Y, Koffas MAG (2006) Biosynthesis of isoprenoids, polyunsaturated fatty acids and flavonoids in Saccharomyces cerevisiae. Microb Cell Fact 5:20. doi:10.1186/1475-2859-5-20
    • (2006) Microb Cell Fact , vol.5 , pp. 20
    • Chemler, J.A.1    Yan, Y.2    Koffas, M.A.G.3
  • 46
    • 48449097118 scopus 로고    scopus 로고
    • Biosynthesis and genetic engineering of proanthocyanidins and (iso)flavonoids
    • COI: 1:CAS:528:DC%2BD1cXptVGksLc%3D
    • Tian L, Pang Y, Dixon RA (2008) Biosynthesis and genetic engineering of proanthocyanidins and (iso)flavonoids. Phytochem Rev 7:445–465. doi:10.1007/s11101-007-9076-y
    • (2008) Phytochem Rev , vol.7 , pp. 445-465
    • Tian, L.1    Pang, Y.2    Dixon, R.A.3
  • 47
    • 78649323531 scopus 로고    scopus 로고
    • Engineered polyketide biosynthesis and biocatalysis in Escherichia coli
    • COI: 1:CAS:528:DC%2BC3cXhsVWqt77O, PID: 20853106
    • Gao X, Wang P, Tang Y (2010) Engineered polyketide biosynthesis and biocatalysis in Escherichia coli. Appl Microbiol Biotechnol 88:1233–1242. doi:10.1007/s00253-010-2860-4
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 1233-1242
    • Gao, X.1    Wang, P.2    Tang, Y.3
  • 48
    • 0036400016 scopus 로고    scopus 로고
    • Dietary flavonoids: bioavailability, metabolic effects, and safety
    • COI: 1:CAS:528:DC%2BD38XmtF2ht7o%3D, PID: 12055336
    • Ross JA, Kasum CM (2002) Dietary flavonoids: bioavailability, metabolic effects, and safety. Annu Rev Nutr 22:19–34. doi:10.1146/annurev.nutr.22.111401.144957
    • (2002) Annu Rev Nutr , vol.22 , pp. 19-34
    • Ross, J.A.1    Kasum, C.M.2
  • 50
    • 84863714863 scopus 로고    scopus 로고
    • Dietary polyphenols as modulators of brain functions: biological actions and molecular mechanisms underpinning their beneficial effects
    • Vauzour D (2012) Dietary polyphenols as modulators of brain functions: biological actions and molecular mechanisms underpinning their beneficial effects. Oxid Med Cell Longev 2012:1–16. doi:10.1155/2012/914273
    • (2012) Oxid Med Cell Longev , vol.2012 , pp. 1-16
    • Vauzour, D.1
  • 51
    • 53649093981 scopus 로고    scopus 로고
    • Structure–activity relationships of flavonoids in the cellular antioxidant activity assay
    • COI: 1:CAS:528:DC%2BD1cXpvVyjt78%3D, PID: 18702468
    • Wolfe KL, Liu RH (2008) Structure–activity relationships of flavonoids in the cellular antioxidant activity assay. J Agric Food Chem 56:8404–8411. doi:10.1021/jf8013074
    • (2008) J Agric Food Chem , vol.56 , pp. 8404-8411
    • Wolfe, K.L.1    Liu, R.H.2
  • 52
  • 53
    • 70450182093 scopus 로고    scopus 로고
    • Polyphenols: food sources, properties and applications—a review
    • El Gharras H (2009) Polyphenols: food sources, properties and applications—a review. Int J Food Sci Technol 44:2512–2518. doi:10.1111/j.1365-2621.2009.02077.x
    • (2009) Int J Food Sci Technol , vol.44 , pp. 2512-2518
    • El Gharras, H.1
  • 55
    • 0034657286 scopus 로고    scopus 로고
    • Proanthocyanidins and tannin-like compounds—nature, occurrence, dietary intake and effects on nutrition and health
    • COI: 1:CAS:528:DC%2BD3cXjsFalsLY%3D
    • Santos-Buelga C, Scalbert A (2000) Proanthocyanidins and tannin-like compounds—nature, occurrence, dietary intake and effects on nutrition and health. J Sci Food Agric 80(7):1094–1117
    • (2000) J Sci Food Agric , vol.80 , Issue.7 , pp. 1094-1117
    • Santos-Buelga, C.1    Scalbert, A.2
  • 56
    • 74049149372 scopus 로고    scopus 로고
    • Advanced separation methods of food anthocyanins, isoflavones and flavanols
    • COI: 1:CAS:528:DC%2BD1MXht1WntLfL, PID: 19691963
    • Valls J, Millán S, Martí MP, Borràs E, Arola L (2009) Advanced separation methods of food anthocyanins, isoflavones and flavanols. J Chromatogr A 1216:7143–7172. doi:10.1016/j.chroma.2009.07.030
    • (2009) J Chromatogr A , vol.1216 , pp. 7143-7172
    • Valls, J.1    Millán, S.2    Martí, M.P.3    Borràs, E.4    Arola, L.5
  • 58
    • 79953117514 scopus 로고    scopus 로고
    • Composition analysis and structural identification of anthocyanins in fruit of waxberry
    • COI: 1:CAS:528:DC%2BC3MXkvFGqtLo%3D
    • Qin CG, Li Y, Niu W, Ding Y, Shang X, Xu C (2011) Composition analysis and structural identification of anthocyanins in fruit of waxberry. Czech J Food Sci 29:171–180
    • (2011) Czech J Food Sci , vol.29 , pp. 171-180
    • Qin, C.G.1    Li, Y.2    Niu, W.3    Ding, Y.4    Shang, X.5    Xu, C.6
  • 59
    • 84875738718 scopus 로고    scopus 로고
    • Anthocyanin-rich purple wheat prolongs the life span of Caenorhabditis elegans probably by activating the DAF-16/FOXO transcription factor
    • COI: 1:CAS:528:DC%2BC3sXjsFejurY%3D, PID: 23470220
    • Chen W, Müller D, Richling E, Wink M (2013) Anthocyanin-rich purple wheat prolongs the life span of Caenorhabditis elegans probably by activating the DAF-16/FOXO transcription factor. J Agric Food Chem 61:3047–3053
    • (2013) J Agric Food Chem , vol.61 , pp. 3047-3053
    • Chen, W.1    Müller, D.2    Richling, E.3    Wink, M.4
  • 60
    • 33745187589 scopus 로고    scopus 로고
    • Polyphenol constituents and antioxidant activity of grape pomace extracts from five Sicilian red grape cultivars
    • COI: 1:CAS:528:DC%2BD28Xmt1agsb8%3D
    • Ruberto G, Renda A, Daquino C, Amico V, Spatafora C, Tringali C, De Tommasi N (2007) Polyphenol constituents and antioxidant activity of grape pomace extracts from five Sicilian red grape cultivars. Food Chem 100:203–210. doi:10.1016/j.foodchem.2005.09.041
    • (2007) Food Chem , vol.100 , pp. 203-210
    • Ruberto, G.1    Renda, A.2    Daquino, C.3    Amico, V.4    Spatafora, C.5    Tringali, C.6    De Tommasi, N.7
  • 61
    • 79952129119 scopus 로고    scopus 로고
    • Protective effects of anthocyanins against amyloid β-peptide-induced damage in neuro-2A cells
    • COI: 1:CAS:528:DC%2BC3MXhs1aitLY%3D, PID: 21302893
    • Shih PH, Wu CH, Yeh CT, Yen GC (2011) Protective effects of anthocyanins against amyloid β-peptide-induced damage in neuro-2A cells. J Agric Food Chem 59:1683–1689. doi:10.1021/jf302972b
    • (2011) J Agric Food Chem , vol.59 , pp. 1683-1689
    • Shih, P.H.1    Wu, C.H.2    Yeh, C.T.3    Yen, G.C.4
  • 62
    • 78650215509 scopus 로고    scopus 로고
    • Regulation of β cleavage of amyloid precursor protein
    • PID: 20882069
    • Wang JF, Lu R, Wang YZ (2010) Regulation of β cleavage of amyloid precursor protein. Neurosci Bull 26:417–427. doi:10.1007/s12264-010-0515-1
    • (2010) Neurosci Bull , vol.26 , pp. 417-427
    • Wang, J.F.1    Lu, R.2    Wang, Y.Z.3
  • 63
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases—new features and familiar faces
    • COI: 1:CAS:528:DC%2BD3MXmsVektbY%3D, PID: 11520976
    • Esler WP, Wolfe MS (2001) A portrait of Alzheimer secretases—new features and familiar faces. Science 293:1449–1454. doi:10.1126/science.1064638
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 64
    • 18044398037 scopus 로고    scopus 로고
    • Alzheimer’s disease: channeling APP to non-amyloidogenic processing
    • COI: 1:CAS:528:DC%2BD2MXjsFGrt78%3D, PID: 15850769
    • Tang BL (2005) Alzheimer’s disease: channeling APP to non-amyloidogenic processing. Biochem Biophys Res Commun 331:375–378. doi:10.1016/j.bbrc.2005.03.074
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 375-378
    • Tang, B.L.1
  • 69
    • 84863201651 scopus 로고    scopus 로고
    • The Psen1-L166P-knock-in mutation leads to amyloid deposition in human wild-type amyloid precursor protein YAC transgenic mice
    • COI: 1:CAS:528:DC%2BC38XhtFartL7L, PID: 22459153
    • Vidal R, Sammeta N, Garringer HJ, Sambamurti K, Miravalle L, Lamb BT, Ghetti B (2012) The Psen1-L166P-knock-in mutation leads to amyloid deposition in human wild-type amyloid precursor protein YAC transgenic mice. Fed Am Soc Exp Biol 26:2899–2910. doi:10.1096/fj.12-205542
    • (2012) Fed Am Soc Exp Biol , vol.26 , pp. 2899-2910
    • Vidal, R.1    Sammeta, N.2    Garringer, H.J.3    Sambamurti, K.4    Miravalle, L.5    Lamb, B.T.6    Ghetti, B.7
  • 70
    • 84878379947 scopus 로고    scopus 로고
    • Previously not recognized deletion in presenilin-1 (p.Leu174del.) in a patient with early-onset familial Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC3sXmvVWhtb4%3D, PID: 23583593
    • Tiedt H, Lueschow A, Winter P, Müller U (2013) Previously not recognized deletion in presenilin-1 (p.Leu174del.) in a patient with early-onset familial Alzheimer’s disease. Neurosci Lett 544:115–118. doi:10.1016/j.neulet.2013.03.056
    • (2013) Neurosci Lett , vol.544 , pp. 115-118
    • Tiedt, H.1    Lueschow, A.2    Winter, P.3    Müller, U.4
  • 71
    • 33748746861 scopus 로고    scopus 로고
    • Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
    • COI: 1:CAS:528:DC%2BD28XovF2js7s%3D, PID: 16846981
    • Spasic D, Tolia A, Dillen K, Baert V, De Strooper B, Vrijens S, Annaert W (2006) Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway. J Biol Chem 281:26569–26577. doi:10.1074/jbc.M600592200
    • (2006) J Biol Chem , vol.281 , pp. 26569-26577
    • Spasic, D.1    Tolia, A.2    Dillen, K.3    Baert, V.4    De Strooper, B.5    Vrijens, S.6    Annaert, W.7
  • 72
    • 0036813113 scopus 로고    scopus 로고
    • Nicotine lowers the secretion of the Alzheimer’s amyloid beta-protein precursor that contains amyloid beta-peptide in rat
    • COI: 1:CAS:528:DC%2BD38XovVGmt7o%3D, PID: 12446972
    • Utsuki T, Shoaib M, Holloway H, Ingram D, Wallace W, Haroutunian V, Sambamurti K, Lahiri D, Greig N (2002) Nicotine lowers the secretion of the Alzheimer’s amyloid beta-protein precursor that contains amyloid beta-peptide in rat. J Alzheimers Dis 4:405
    • (2002) J Alzheimers Dis , vol.4 , pp. 405
    • Utsuki, T.1    Shoaib, M.2    Holloway, H.3    Ingram, D.4    Wallace, W.5    Haroutunian, V.6    Sambamurti, K.7    Lahiri, D.8    Greig, N.9
  • 73
    • 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
    • COI: 1:CAS:528:DC%2BD2sXot1WqsQ%3D%3D, PID: 17253770
    • Hirohata M, Hasegawa K, Tsutsumi-Yasuhara S, Ohhashi Y, Ookoshi T, Ono K, Yamada M, Naiki H (2007) 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 46:1888–1899. doi:10.1021/bi061540x
    • (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
  • 74
    • 84870057502 scopus 로고    scopus 로고
    • The binding of resveratrol to monomer and fibril amyloid beta
    • COI: 1:CAS:528:DC%2BC38XhsVOgsb3P, PID: 22981725
    • Ge JF, Qiao JP, Qi CC, Wang CW, Zhou JN (2012) The binding of resveratrol to monomer and fibril amyloid beta. Neurochem Int 61:1192–1201. doi:10.1016/j.neuint.2012.08.012
    • (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
  • 75
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism
    • COI: 1:CAS:528:DC%2BD28XhsVSjt7g%3D, PID: 16492146
    • Porat Y, Abramowitz A, Gazit E (2006) Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des 67:27–37. doi:10.1111/j.1747-0285.2005.00318.x
    • (2006) Chem Biol Drug Des , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 76
    • 77953290521 scopus 로고    scopus 로고
    • Molecular docking studies of phlorotannins from Eisenia bicyclis with BACE1 inhibitory activity
    • COI: 1:CAS:528:DC%2BC3cXmsVOhtr8%3D, PID: 20462757
    • Jung HA, Oh SH, Choi JS (2010) Molecular docking studies of phlorotannins from Eisenia bicyclis with BACE1 inhibitory activity. Bioorg Med Chem Lett 20:3211–3215. doi:10.1016/j.bmcl.2010.04.093
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 3211-3215
    • Jung, H.A.1    Oh, S.H.2    Choi, J.S.3
  • 78
    • 84862850617 scopus 로고    scopus 로고
    • Regulation of alpha-secretase ADAM10 expression and activity
    • COI: 1:CAS:528:DC%2BC38XksVeqt7g%3D, PID: 21969210
    • Endres K, Fahrenholz F (2012) Regulation of alpha-secretase ADAM10 expression and activity. Exp Brain Res 217:343–352. doi:10.1007/s00221-011-2885-7
    • (2012) Exp Brain Res , vol.217 , pp. 343-352
    • Endres, K.1    Fahrenholz, F.2
  • 79
    • 77949595824 scopus 로고    scopus 로고
    • Upregulation of the α-secretase ADAM10—risk or reason for hope?
    • COI: 1:CAS:528:DC%2BC3cXktFOnt7Y%3D
    • Endres K, Fahrenholz F (2010) Upregulation of the α-secretase ADAM10—risk or reason for hope? Fed Eur Biochem Soc J 277:1585–1596. doi:10.1111/j.1742-4658.2010.07566.x
    • (2010) Fed Eur Biochem Soc J , vol.277 , pp. 1585-1596
    • Endres, K.1    Fahrenholz, F.2
  • 80
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the trans-golgi network
    • COI: 1:CAS:528:DC%2BD3cXpvFChuw%3D%3D, PID: 10644715
    • Skovronsky DM, Moore DB, Milla ME, Doms RW, Lee VM (2000) Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the trans-golgi network. J Biol Chem 275:2568–2575
    • (2000) J Biol Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 81
    • 77649083093 scopus 로고    scopus 로고
    • Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors
    • PID: 20151049
    • Tian S, Jianhua W (2010) Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors. Int J Biol Sci 6:89–95
    • (2010) Int J Biol Sci , vol.6 , pp. 89-95
    • Tian, S.1    Jianhua, W.2
  • 82
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases
    • COI: 1:CAS:528:DC%2BD3MXmsFejsL8%3D
    • Anders A, Gilbert S, Garten W, Postina R, Fahrenholz F (2001) Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases. Fed Am Soc Exp Biol J 15:1837–1839. doi:10.1096/fj.01
    • (2001) Fed Am Soc Exp Biol J , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 83
    • 52949099119 scopus 로고    scopus 로고
    • The ADAM metalloproteinases
    • COI: 1:CAS:528:DC%2BD1cXht1ShsLnM, PID: 18762209
    • Edwards DR, Handsley MM, Pennington CJ (2008) The ADAM metalloproteinases. Mol Aspects Med 29:258–289. doi:10.1016/j.mam.2008.08.001
    • (2008) Mol Aspects Med , vol.29 , pp. 258-289
    • Edwards, D.R.1    Handsley, M.M.2    Pennington, C.J.3
  • 84
    • 0033607676 scopus 로고    scopus 로고
    • The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity
    • COI: 1:CAS:528:DyaK1MXnslOltbk%3D, PID: 10567353
    • Zhong M, Munzer JS, Basak A, Benjannet S, Mowla SJ, Decroly E, Chrétien M, Seidah NG (1999) The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity. J Biol Chem 274:33913–33920
    • (1999) J Biol Chem , vol.274 , pp. 33913-33920
    • Zhong, M.1    Munzer, J.S.2    Basak, A.3    Benjannet, S.4    Mowla, S.J.5    Decroly, E.6    Chrétien, M.7    Seidah, N.G.8
  • 85
    • 84870357798 scopus 로고    scopus 로고
    • Phlorotannin-rich Ecklonia cava reduces the production of beta-amyloid by modulating alpha- and gamma-secretase expression and activity
    • COI: 1:CAS:528:DC%2BC3sXhs1ersrc%3D, PID: 23041113
    • Kang IJ, Jang BG, In S, Choi B, Kim M, Kim MJ (2013) Phlorotannin-rich Ecklonia cava reduces the production of beta-amyloid by modulating alpha- and gamma-secretase expression and activity. Neurotoxicology 34:16–24. doi:10.1016/j.neuro.2012.09.013
    • (2013) Neurotoxicology , vol.34 , pp. 16-24
    • Kang, I.J.1    Jang, B.G.2    In, S.3    Choi, B.4    Kim, M.5    Kim, M.J.6
  • 86
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice
    • COI: 1:CAS:528:DC%2BD2MXhtVGls73F, PID: 16177050
    • Rezai-Zadeh K, Shytle D, Sun N, Mori T, Hou H, Jeanniton D, Ehrhart J, Townsend K, Zeng J, Morgan D, Hardy J, Town T, Tan J (2005) Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J Neurosci 25:8807–8814. doi:10.1523/JNEUROSCI.1521-05.2005
    • (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    Hardy, J.11    Town, T.12    Tan, J.13
  • 87
    • 33750807197 scopus 로고    scopus 로고
    • Pomegranate juice decreases amyloid load and improves behavior in a mouse model of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD28Xht1Cmt7rP, PID: 17010630
    • Hartman RE, Shah A, Fagan AM, Schwetye KE, Parsadanian M, Schulman RN, Finn MB, Holtzman DM (2006) Pomegranate juice decreases amyloid load and improves behavior in a mouse model of Alzheimer’s disease. Neurobiol Dis 24:506–515. doi:10.1016/j.nbd.2006.08.006
    • (2006) Neurobiol Dis , vol.24 , pp. 506-515
    • Hartman, R.E.1    Shah, A.2    Fagan, A.M.3    Schwetye, K.E.4    Parsadanian, M.5    Schulman, R.N.6    Finn, M.B.7    Holtzman, D.M.8
  • 88
    • 0344507324 scopus 로고    scopus 로고
    • Protein kinase C and amyloid precursor protein processing in skin fibroblasts from sporadic and familial Alzheimer’s disease cases
    • COI: 1:CAS:528:DyaK1MXitFWrsL0%3D, PID: 10101252
    • Vestling M, Cedazo-Mínguez Á, Adem A, Wiehager B, Racchi M, Lannfelt L, Cowburn RF (1999) Protein kinase C and amyloid precursor protein processing in skin fibroblasts from sporadic and familial Alzheimer’s disease cases. Biochim Biophys Acta 1453:341–350
    • (1999) Biochim Biophys Acta , vol.1453 , pp. 341-350
    • Vestling, M.1    Cedazo-Mínguez, Á.2    Adem, A.3    Wiehager, B.4    Racchi, M.5    Lannfelt, L.6    Cowburn, R.F.7
  • 90
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against Aβ toxicity and PKC-dependent release of non-amyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • COI: 1:CAS:528:DC%2BD3sXjsFakt74%3D
    • Levites Y, Amit T, Mandel S, Youdim MBH (2003) Neuroprotection and neurorescue against Aβ toxicity and PKC-dependent release of non-amyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. Fed Am Soc Exp Biol J 17:952–958
    • (2003) Fed Am Soc Exp Biol J , vol.17 , pp. 952-958
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.H.4
  • 91
    • 84942303229 scopus 로고    scopus 로고
    • Beta-secretase as a target for Alzheimer’s disease drug discovery: an overview of in vitro methods for characterization of inhibitors
    • COI: 1:CAS:528:DC%2BC3MXkvVaqs70%3D, PID: 21503735
    • Mancini F, De Simone A, Andrisano V (2011) Beta-secretase as a target for Alzheimer’s disease drug discovery: an overview of in vitro methods for characterization of inhibitors. Anal Bioanal Chem 400:1979–1996. doi:10.1007/s00216-011-4963-x
    • (2011) Anal Bioanal Chem , vol.400 , pp. 1979-1996
    • Mancini, F.1    De Simone, A.2    Andrisano, V.3
  • 92
    • 44349184966 scopus 로고    scopus 로고
    • Crystal structure of an active form of BACE1, an enzyme responsible for amyloid β protein production
    • COI: 1:CAS:528:DC%2BD1cXms1elsro%3D, PID: 18378702
    • Shimizu H, Tosaki A, Kaneko K, Hisano T, Sakurai T, Nukina N (2008) Crystal structure of an active form of BACE1, an enzyme responsible for amyloid β protein production. Mol Cell Biol 28:3663–3671. doi:10.1128/MCB.02185-07
    • (2008) Mol Cell Biol , vol.28 , pp. 3663-3671
    • Shimizu, H.1    Tosaki, A.2    Kaneko, K.3    Hisano, T.4    Sakurai, T.5    Nukina, N.6
  • 93
    • 33751504561 scopus 로고    scopus 로고
    • Assigning the protonation states of the key aspartates in β-secretase using QM/MM X-ray structure refinement
    • COI: 1:CAS:528:DC%2BD28XltlSnu7g%3D, PID: 19079786
    • Yu N, Hayik SA, Wang B, Liao N, Reynolds CH, Merz KM (2006) Assigning the protonation states of the key aspartates in β-secretase using QM/MM X-ray structure refinement. J Chem Theory Comput 2:1057–1069. doi:10.1021/ct0600060
    • (2006) J Chem Theory Comput , vol.2 , pp. 1057-1069
    • Yu, N.1    Hayik, S.A.2    Wang, B.3    Liao, N.4    Reynolds, C.H.5    Merz, K.M.6
  • 95
    • 79956215028 scopus 로고    scopus 로고
    • Conformational transition in the substrate binding domain of β-secretase exploited by NMA and its implication in inhibitor recognition: BACE1-myricetin a case study
    • COI: 1:CAS:528:DC%2BC3MXmsVCjurw%3D, PID: 21354237
    • Chakraborty S, Kumar S, Basu S (2011) Conformational transition in the substrate binding domain of β-secretase exploited by NMA and its implication in inhibitor recognition: BACE1-myricetin a case study. Neurochem Int 58:914–923. doi:10.1016/j.neuint.2011.02.021
    • (2011) Neurochem Int , vol.58 , pp. 914-923
    • Chakraborty, S.1    Kumar, S.2    Basu, S.3
  • 96
    • 0035968334 scopus 로고    scopus 로고
    • Mechanism of inhibition of β-site amyloid precursor protein-cleaving enzyme (BACE) by a statine-based peptide
    • COI: 1:CAS:528:DC%2BD3MXltVWjur8%3D, PID: 11306583
    • Marcinkeviciene J, Luo Y, Graciani NR, Combs AP, Copeland RA (2001) Mechanism of inhibition of β-site amyloid precursor protein-cleaving enzyme (BACE) by a statine-based peptide. J Biol Chem 276:23790–23794. doi:10.1074/jbc.M101896200
    • (2001) J Biol Chem , vol.276 , pp. 23790-23794
    • Marcinkeviciene, J.1    Luo, Y.2    Graciani, N.R.3    Combs, A.P.4    Copeland, R.A.5
  • 97
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer’s disease—proteolysis holds the key
    • COI: 1:CAS:528:DyaK1MXntFaktr0%3D, PID: 10542139
    • Haass C, De Strooper B (1999) The presenilins in Alzheimer’s disease—proteolysis holds the key. Science 286:916–919. doi:10.1126/science.286.5441.916
    • (1999) Science , vol.286 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 98
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for π-stacking in the self-assembly of amyloid fibrils
    • COI: 1:CAS:528:DC%2BD38Xlsleguw%3D%3D
    • Gazit E (2002) A possible role for π-stacking in the self-assembly of amyloid fibrils. Fed Am Soc Exp Biol J 16:77–83. doi:10.1096/fj.01-0442hyp
    • (2002) Fed Am Soc Exp Biol J , vol.16 , pp. 77-83
    • Gazit, E.1
  • 99
    • 84858758039 scopus 로고    scopus 로고
    • An azobenzene photoswitch sheds light on turn nucleation in amyloid-β self-assembly
    • COI: 1:CAS:528:DC%2BC38XktlOksQ%3D%3D, PID: 22860190
    • Doran TM, Anderson EA, Latchney SE, Opanashuk LA, Nilsson BL (2012) An azobenzene photoswitch sheds light on turn nucleation in amyloid-β self-assembly. ACS Chem Neurosci 3:211–220. doi:10.1021/cn2001188
    • (2012) ACS Chem Neurosci , vol.3 , pp. 211-220
    • Doran, T.M.1    Anderson, E.A.2    Latchney, S.E.3    Opanashuk, L.A.4    Nilsson, B.L.5
  • 100
    • 77956685965 scopus 로고    scopus 로고
    • Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α, α-disubstitution results in altered aggregate size and morphology
    • COI: 1:CAS:528:DC%2BC3cXosFCmtbc%3D, PID: 22778850
    • Bett CK, Ngunjiri JN, Serem WK, Fontenot KR, Hammer RP, McCarley RL, Garno JC (2010) Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α, α-disubstitution results in altered aggregate size and morphology. ACS Chem Neurosci 1:608–626. doi:10.1021/cn100045q
    • (2010) ACS Chem Neurosci , vol.1 , pp. 608-626
    • Bett, C.K.1    Ngunjiri, J.N.2    Serem, W.K.3    Fontenot, K.R.4    Hammer, R.P.5    McCarley, R.L.6    Garno, J.C.7
  • 101
    • 84874639389 scopus 로고    scopus 로고
    • Molecular structures of amyloid and prion fibrils: consensus versus controversy
    • COI: 1:CAS:528:DC%2BC3sXktFSktw%3D%3D, PID: 23294335
    • Tycko R, Wickner RB (2013) Molecular structures of amyloid and prion fibrils: consensus versus controversy. Acc Chem Res 46:1487–1496. doi:10.1021/ar300282r
    • (2013) Acc Chem Res , vol.46 , pp. 1487-1496
    • Tycko, R.1    Wickner, R.B.2
  • 102
    • 84879744934 scopus 로고    scopus 로고
    • Tanshinones inhibit amyloid aggregation by amyloid-β peptide, disaggregate amyloid fibrils, and protect cultured cells
    • COI: 1:CAS:528:DC%2BC3sXktF2it7g%3D, PID: 23506133
    • Wang Q, Yu X, Patal K, Hu R, Chuang S, Zhang G, Zheng J (2013) Tanshinones inhibit amyloid aggregation by amyloid-β peptide, disaggregate amyloid fibrils, and protect cultured cells. ACS Chem Neurosci 4:1004–1015. doi:10.1021/cn400051e
    • (2013) ACS Chem Neurosci , vol.4 , pp. 1004-1015
    • Wang, Q.1    Yu, X.2    Patal, K.3    Hu, R.4    Chuang, S.5    Zhang, G.6    Zheng, J.7
  • 103
    • 0030133644 scopus 로고    scopus 로고
    • Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides
    • COI: 1:CAS:528:DyaK28XjvVKmtLw%3D, PID: 8807864
    • Ashburn TT, Han H, McGuinness BF, Lansbury PT (1996) Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides. Chem Biol 3:351–358
    • (1996) Chem Biol , vol.3 , pp. 351-358
    • Ashburn, T.T.1    Han, H.2    McGuinness, B.F.3    Lansbury, P.T.4
  • 104
    • 33846126930 scopus 로고    scopus 로고
    • Plasticity of amyloid fibrils
    • COI: 1:CAS:528:DC%2BD28XhtlSgs77J, PID: 17198370
    • Wetzel R, Shivaprasad S, Williams AD (2007) Plasticity of amyloid fibrils. Biochemistry 46:1–10
    • (2007) Biochemistry , vol.46 , pp. 1-10
    • Wetzel, R.1    Shivaprasad, S.2    Williams, A.D.3
  • 105
    • 84883217920 scopus 로고    scopus 로고
    • Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils
    • COI: 1:CAS:528:DC%2BC3sXotVSmu78%3D, PID: 23701594
    • Ma J, Komatsu H, Kim YS, Liu L, Hochstrasser RM, Axelsen PH (2013) Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils. ACS Chem Neurosci 4:1236–1243. doi:10.1021/cn400092v
    • (2013) ACS Chem Neurosci , vol.4 , pp. 1236-1243
    • Ma, J.1    Komatsu, H.2    Kim, Y.S.3    Liu, L.4    Hochstrasser, R.M.5    Axelsen, P.H.6
  • 106
    • 84887624150 scopus 로고    scopus 로고
    • Frontiers in the pathogenesis of Alzheimer’s disease
    • PID: 21416019
    • Sambamurti K, Rao KS, Pappolla MA (2009) Frontiers in the pathogenesis of Alzheimer’s disease. Indian J Psychiatry 51:S56–S60
    • (2009) Indian J Psychiatry , vol.51 , pp. S56-S60
    • Sambamurti, K.1    Rao, K.S.2    Pappolla, M.A.3
  • 107
    • 77958487672 scopus 로고    scopus 로고
    • Effects of peptides derived from terminal modifications of the Aβ central hydrophobic core on Aβ fibrillization
    • COI: 1:CAS:528:DC%2BC3cXhtVKrsL3E, PID: 22778807
    • Bett CK, Serem WK, Fontenot KR, Hammer RP, Garno JC (2010) Effects of peptides derived from terminal modifications of the Aβ central hydrophobic core on Aβ fibrillization. ACS Chem Neurosci 1:661–678. doi:10.1021/cn900019r
    • (2010) ACS Chem Neurosci , vol.1 , pp. 661-678
    • Bett, C.K.1    Serem, W.K.2    Fontenot, K.R.3    Hammer, R.P.4    Garno, J.C.5
  • 108
    • 84860834940 scopus 로고    scopus 로고
    • The role of Pro, Gly Lys, and Arg containing peptides on amyloid-beta aggregation
    • Jagota S, Rajadas J (2011) The role of Pro, Gly Lys, and Arg containing peptides on amyloid-beta aggregation. Int J Pept Res Ther 18:53–61. doi:10.1007/s10989-011-9278-4
    • (2011) Int J Pept Res Ther , vol.18 , pp. 53-61
    • Jagota, S.1    Rajadas, J.2
  • 109
    • 84868542498 scopus 로고    scopus 로고
    • Liberation of copper from amyloid plaques: making a risk factor useful for Alzheimer’s disease treatment
    • COI: 1:CAS:528:DC%2BC38XnvF2nsLY%3D, PID: 22663067
    • Geng J, Li M, Wu L, Ren J, Qu X (2012) Liberation of copper from amyloid plaques: making a risk factor useful for Alzheimer’s disease treatment. J Med Chem 55:9146–9155. doi:10.1021/jm3003813
    • (2012) J Med Chem , vol.55 , pp. 9146-9155
    • Geng, J.1    Li, M.2    Wu, L.3    Ren, J.4    Qu, X.5
  • 110
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogensis of Alzheimer’s disease: significance of monomeric, oligomeric and fibrillar Aβ
    • COI: 1:CAS:528:DC%2BD2MXotFaktr0%3D, PID: 15709478
    • Glabe CC (2005) Amyloid accumulation and pathogensis of Alzheimer’s disease: significance of monomeric, oligomeric and fibrillar Aβ. Subcell Biochem 38:167–177
    • (2005) Subcell Biochem , vol.38 , pp. 167-177
    • Glabe, C.C.1
  • 112
    • 36348958392 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of S-allyl-L-cysteine and its activity to destabilize Alzheimer’s β-amyloid fibrils in vitro
    • COI: 1:CAS:528:DC%2BD2sXhtlykur%2FI, PID: 18023978
    • Gupta VB, Rao KS (2007) Anti-amyloidogenic activity of S-allyl-L-cysteine and its activity to destabilize Alzheimer’s β-amyloid fibrils in vitro. Neurosci Lett 429:75–80. doi:10.1016/j.neulet.2007.09.042
    • (2007) Neurosci Lett , vol.429 , pp. 75-80
    • Gupta, V.B.1    Rao, K.S.2
  • 114
    • 77955680341 scopus 로고    scopus 로고
    • A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation
    • COI: 1:CAS:528:DC%2BC3cXptlynsb0%3D, PID: 20666485
    • Yamaguchi T, Yagi H, Goto Y, Matsuzaki K, Hoshino M (2010) A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation. Biochemistry 49:7100–7107
    • (2010) Biochemistry , vol.49 , pp. 7100-7107
    • Yamaguchi, T.1    Yagi, H.2    Goto, Y.3    Matsuzaki, K.4    Hoshino, M.5
  • 115
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer’s disease: strategies for disease modification
    • COI: 1:CAS:528:DC%2BC3cXlsVWjsrw%3D, PID: 20431570
    • Citron M (2010) Alzheimer’s disease: strategies for disease modification. Nat Rev Drug Discov 9:387–398. doi:10.1038/nrd2896
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 387-398
    • Citron, M.1
  • 116
    • 77951681963 scopus 로고    scopus 로고
    • Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation
    • COI: 1:CAS:528:DC%2BC3cXhtFansLk%3D, PID: 22778827
    • Cabaleiro-Lago C, Quinlan-Pluck F, Lynch I, Dawson KA, Linse S (2010) Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation. ACS Chem Neurosci 1:279–287. doi:10.1021/cn900027u
    • (2010) ACS Chem Neurosci , vol.1 , pp. 279-287
    • Cabaleiro-Lago, C.1    Quinlan-Pluck, F.2    Lynch, I.3    Dawson, K.A.4    Linse, S.5
  • 117
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • COI: 1:CAS:528:DC%2BD2sXjs1Sitb4%3D, PID: 17284452
    • Necula M, Kayed R, Milton S, Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282:10311–10324. doi:10.1074/jbc.M608207200
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 118
    • 80054979271 scopus 로고    scopus 로고
    • Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease
    • COI: 1:CAS:528:DC%2BC3MXht1Giu7vE, PID: 21857114
    • Chaudhary N, Singh S, Nagaraj R (2011) Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease. J Biosci 36:679–689. doi:10.1007/s12038-011-9104-3
    • (2011) J Biosci , vol.36 , pp. 679-689
    • Chaudhary, N.1    Singh, S.2    Nagaraj, R.3
  • 119
    • 84862848514 scopus 로고    scopus 로고
    • A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity
    • COI: 1:CAS:528:DC%2BC38XktFWhs7s%3D, PID: 22860216
    • Sinha S, Lopes DHJ, Bitan G (2012) A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity. ACS Chem Neurosci 3:473–481
    • (2012) ACS Chem Neurosci , vol.3 , pp. 473-481
    • Sinha, S.1    Lopes, D.H.J.2    Bitan, G.3
  • 120
    • 48349093043 scopus 로고    scopus 로고
    • Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry
    • COI: 1:CAS:528:DC%2BD1cXps1WlsbY%3D, PID: 18448354
    • Bazoti FN, Bergquist J, Markides K, Tsarbopoulos A (2008) Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry. J Am Soc Mass Spectrom 19:1078–1085. doi:10.1016/j.jasms.2008.03.011
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1078-1085
    • Bazoti, F.N.1    Bergquist, J.2    Markides, K.3    Tsarbopoulos, A.4
  • 121
    • 69349098271 scopus 로고    scopus 로고
    • (−)-Epigallocatechin-3-Gallate (EGCG) maintains κ-casein in its pre-fibrillar state without redirecting its aggregation pathway
    • COI: 1:CAS:528:DC%2BD1MXhtV2ku7rO, PID: 19616561
    • Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA (2009) (−)-Epigallocatechin-3-Gallate (EGCG) maintains κ-casein in its pre-fibrillar state without redirecting its aggregation pathway. J Mol Biol 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
  • 122
    • 84555177564 scopus 로고    scopus 로고
    • Clicked” sugar–curcumin conjugate: modulator of amyloid-β and tau peptide aggregation at ultralow concentrations
    • COI: 1:CAS:528:DC%2BC3MXhtlKjs7zP, PID: 22860163
    • Dolai S, Shi W, Corbo C, Sun C, Averick S, Obeysekera D, Farid M, Alonso A, Banerjee P, Raja K (2011) “Clicked” sugar–curcumin conjugate: modulator of amyloid-β and tau peptide aggregation at ultralow concentrations. ACS Chem Neurosci 2:694–699
    • (2011) ACS Chem Neurosci , vol.2 , pp. 694-699
    • Dolai, S.1    Shi, W.2    Corbo, C.3    Sun, C.4    Averick, S.5    Obeysekera, D.6    Farid, M.7    Alonso, A.8    Banerjee, P.9    Raja, K.10
  • 123
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions
    • COI: 1:CAS:528:DC%2BD2cXos1WjtLY%3D, PID: 15533050
    • Porat Y, Mazor Y, Efrat S, Gazit E (2004) Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 43:14454–14462
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 124
    • 63449131863 scopus 로고    scopus 로고
    • 9,10-Anthraquinone hinders beta β-aggregation: how does a small molecule interfere with Aβ-peptide amyloid fibrillation?
    • COI: 1:CAS:528:DC%2BD1MXms1ags7k%3D, PID: 19309732
    • Convertino M, Pellarin R, Catto M, Carotti A, Caflisch A (2009) 9,10-Anthraquinone hinders beta β-aggregation: how does a small molecule interfere with Aβ-peptide amyloid fibrillation? Protein Sci 18:792–800. doi:10.1002/pro.87
    • (2009) Protein Sci , vol.18 , pp. 792-800
    • Convertino, M.1    Pellarin, R.2    Catto, M.3    Carotti, A.4    Caflisch, A.5
  • 125
    • 64249166299 scopus 로고    scopus 로고
    • The polyphenol piceid destabilizes preformed amyloid fibrils and oligomers in vitro: hypothesis on possible molecular mechanisms
    • PID: 19030989
    • Rivière C, Delaunay JC, Immel F, Cullin C, Monti JP (2009) The polyphenol piceid destabilizes preformed amyloid fibrils and oligomers in vitro: hypothesis on possible molecular mechanisms. Neurochem Res 34:1120–1128. doi:10.1007/s11064-008-9883-6
    • (2009) Neurochem Res , vol.34 , pp. 1120-1128
    • Rivière, C.1    Delaunay, J.C.2    Immel, F.3    Cullin, C.4    Monti, J.P.5
  • 126
    • 81455136028 scopus 로고    scopus 로고
    • A safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregates
    • COI: 1:CAS:528:DC%2BC3MXht1WksL7O, PID: 22860159
    • Wong HE, Qi W, Choi HM, Fernandez EJ, Kwon I (2011) A safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregates. ACS Chem Neurosci 2:645–657. doi:10.1021/cn200056g
    • (2011) ACS Chem Neurosci , vol.2 , pp. 645-657
    • Wong, H.E.1    Qi, W.2    Choi, H.M.3    Fernandez, E.J.4    Kwon, I.5
  • 127
    • 83055178978 scopus 로고    scopus 로고
    • Apricot carotenoids possess potent anti-amyloidogenic activity in vitro
    • COI: 1:CAS:528:DC%2BC3MXhtl2ntr7L, PID: 22043804
    • Katayama S, Ogawa H, Nakamura S (2011) Apricot carotenoids possess potent anti-amyloidogenic activity in vitro. J Agric Food Chem 59:12691–12696. doi:10.1021/jf203654c
    • (2011) J Agric Food Chem , vol.59 , pp. 12691-12696
    • Katayama, S.1    Ogawa, H.2    Nakamura, S.3
  • 128
    • 70349750314 scopus 로고    scopus 로고
    • Consumption of grape seed extract prevents amyloid-β deposition and attenuates inflammation in brain of an Alzheimer’s disease mouse
    • PID: 19384583
    • Wang YJ, Thomas P, Zhong JH, Bi FF, Kosaraju S, Pollard A, Fenech M, Zhou XF (2009) Consumption of grape seed extract prevents amyloid-β deposition and attenuates inflammation in brain of an Alzheimer’s disease mouse. Neurotox Res 15:3–14. doi:10.1007/s12640-009-9000-x
    • (2009) Neurotox Res , vol.15 , pp. 3-14
    • Wang, Y.J.1    Thomas, P.2    Zhong, J.H.3    Bi, F.F.4    Kosaraju, S.5    Pollard, A.6    Fenech, M.7    Zhou, X.F.8
  • 129
    • 84882585441 scopus 로고    scopus 로고
    • Critical evaluation of biodegradable polymers used in nanodrugs
    • PID: 23990720
    • Marin E, Briceño MI, Caballero-George C (2013) Critical evaluation of biodegradable polymers used in nanodrugs. Int J Nanomedicine 8:3071–3091. doi:10.2147/IJN.S47186
    • (2013) Int J Nanomedicine , vol.8 , pp. 3071-3091
    • Marin, E.1    Briceño, M.I.2    Caballero-George, C.3
  • 130
    • 71249124418 scopus 로고    scopus 로고
    • Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation
    • COI: 1:CAS:528:DC%2BD1MXhsFaiur%2FP, PID: 19744518
    • Feng Y, Wang XP, Yang SG, Wang YJ, Zhang X, Du XT, Sun XX, Zhao M, Huang L, Liu RT (2009) Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation. Neurotoxicology 30:986–995. doi:10.1016/j.neuro.2009.08.013
    • (2009) Neurotoxicology , vol.30 , pp. 986-995
    • Feng, Y.1    Wang, X.P.2    Yang, S.G.3    Wang, Y.J.4    Zhang, X.5    Du, X.T.6    Sun, X.X.7    Zhao, M.8    Huang, L.9    Liu, R.T.10
  • 131
    • 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
    • COI: 1:CAS:528:DC%2BD3sXotFSktr8%3D, PID: 12969264
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M (2003) Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer’s disease. J Neurochem 87:172–181. doi:10.1046/j.1471-4159.2003.01976.x
    • (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
  • 133
    • 54049103538 scopus 로고    scopus 로고
    • Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS
    • COI: 1:CAS:528:DC%2BD1cXht12kur%2FJ, PID: 18778797
    • Shoval H, Weiner L, Gazit E, Levy M, Pinchuk I, Lichtenberg D (2008) Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS. Biochim Biophys Acta 1784:1570–1577. doi:10.1016/j.bbapap.2008.08.007
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1570-1577
    • Shoval, H.1    Weiner, L.2    Gazit, E.3    Levy, M.4    Pinchuk, I.5    Lichtenberg, D.6
  • 134
    • 52049102256 scopus 로고    scopus 로고
    • Structural requirements for the flavonoid fisetin in inhibiting fibril formation of amyloid β protein
    • COI: 1:CAS:528:DC%2BD1cXhtFersb%2FK, PID: 18761054
    • Akaishi T, Morimoto T, Shibao M, Watanabe S, Sakai-Kato K, Utsunomiya-Tate N, Abe K (2008) Structural requirements for the flavonoid fisetin in inhibiting fibril formation of amyloid β protein. Neurosci Lett 444:280–285. doi:10.1016/j.neulet.2008.08.052
    • (2008) Neurosci Lett , vol.444 , pp. 280-285
    • Akaishi, T.1    Morimoto, T.2    Shibao, M.3    Watanabe, S.4    Sakai-Kato, K.5    Utsunomiya-Tate, N.6    Abe, K.7
  • 135
    • 77957163779 scopus 로고    scopus 로고
    • Soy isoflavones as potential inhibitors of Alzheimer β-amyloid fibril aggregation in vitro
    • COI: 1:CAS:528:DC%2BC3cXht1CiurvE
    • Henry-Vitrac C, Berbille H, Mérillon JM, Vitrac X (2010) Soy isoflavones as potential inhibitors of Alzheimer β-amyloid fibril aggregation in vitro. Food Res Int 43:2176–2178. doi:10.1016/j.foodres.2010.07.032
    • (2010) Food Res Int , vol.43 , pp. 2176-2178
    • Henry-Vitrac, C.1    Berbille, H.2    Mérillon, J.M.3    Vitrac, X.4
  • 136
    • 72049085497 scopus 로고    scopus 로고
    • Carboxymethylated-k-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation
    • COI: 1:CAS:528:DC%2BD1MXhsFykurrE, PID: 19931462
    • Carver JA, Duggan PJ, Ecroyd H, Liu Y, Meyer AG, Tranberg CE (2010) Carboxymethylated-k-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation. Bioorg Med Chem 18:222–228. doi:10.1016/j.bmc.2009.10.063
    • (2010) Bioorg Med Chem , vol.18 , pp. 222-228
    • Carver, J.A.1    Duggan, P.J.2    Ecroyd, H.3    Liu, Y.4    Meyer, A.G.5    Tranberg, C.E.6
  • 137
    • 33845334891 scopus 로고    scopus 로고
    • Inhibitory activity of stilbenes on Alzheimer’s β-amyloid fibrils in vitro
    • PID: 17049256
    • Rivière C, Richard T, Quentin L, Krisa S, Mérillon JM, Monti JP (2007) Inhibitory activity of stilbenes on Alzheimer’s β-amyloid fibrils in vitro. Bioorg Med Chem 15:1160–1167. doi:10.1016/j.bmc.2006.09.069
    • (2007) Bioorg Med Chem , vol.15 , pp. 1160-1167
    • Rivière, C.1    Richard, T.2    Quentin, L.3    Krisa, S.4    Mérillon, J.M.5    Monti, J.P.6
  • 139
    • 33745173188 scopus 로고    scopus 로고
    • Anti-amyloidogenic effects of antioxidants: implications for the prevention and therapeutics of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD28XlvF2itbg%3D, PID: 16644188
    • Ono K, Hamaguchi T, Naiki H, Yamada M (2006) Anti-amyloidogenic effects of antioxidants: implications for the prevention and therapeutics of Alzheimer’s disease. Biochim Biophys Acta 1762:575–586. doi:10.1016/j.bbadis.2006.03.002
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 575-586
    • Ono, K.1    Hamaguchi, T.2    Naiki, H.3    Yamada, M.4
  • 140
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer’s β-amyloid fibrils in vitro
    • COI: 1:CAS:528:DC%2BD2cXptFOktbc%3D, PID: 15511626
    • Ono K, Hasegawa K, Naiki H, Yamada M (2004) Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer’s β-amyloid fibrils in vitro. Biochim Biophys Acta 1690:193–202
    • (2004) Biochim Biophys Acta , vol.1690 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 141
    • 33644945380 scopus 로고    scopus 로고
    • Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro
    • COI: 1:CAS:528:DC%2BD28Xjslars7c%3D, PID: 16524383
    • Ono K, Yamada M (2006) Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro. J Neurochem 97:105–115. doi:10.1111/j.1471-4159.2006.03707.x
    • (2006) J Neurochem , vol.97 , pp. 105-115
    • Ono, K.1    Yamada, M.2
  • 142
    • 33750853036 scopus 로고    scopus 로고
    • The development of preventives and therapeutics for Alzheimer’s disease that inhibit the formation of β-amyloid fibrils (fAβ), as well as destabilize preformed fAβ
    • COI: 1:CAS:528:DC%2BD28Xht1GntrbP, PID: 17105432
    • Ono K, Naiki H, Yamada M (2006) The development of preventives and therapeutics for Alzheimer’s disease that inhibit the formation of β-amyloid fibrils (fAβ), as well as destabilize preformed fAβ. Curr Pharm Des 12:4357–4375
    • (2006) Curr Pharm Des , vol.12 , pp. 4357-4375
    • Ono, K.1    Naiki, H.2    Yamada, M.3
  • 143
    • 79956203739 scopus 로고    scopus 로고
    • Protective effect of ε-viniferin on β-amyloid peptide aggregation investigated by electrospray ionization mass spectrometry
    • COI: 1:CAS:528:DC%2BC3MXlvVOns7Y%3D, PID: 21524590
    • Richard T, Poupard P, Nassra M, Papastamoulis Y, Iglésias ML, Krisa S, Waffo-Teguo P, Mérillon JM, Monti JP (2011) Protective effect of ε-viniferin on β-amyloid peptide aggregation investigated by electrospray ionization mass spectrometry. Bioorg Med Chem 19:3152–3155. doi:10.1016/j.bmc.2011.04.001
    • (2011) Bioorg Med Chem , vol.19 , pp. 3152-3155
    • Richard, T.1    Poupard, P.2    Nassra, M.3    Papastamoulis, Y.4    Iglésias, M.L.5    Krisa, S.6    Waffo-Teguo, P.7    Mérillon, J.M.8    Monti, J.P.9
  • 144
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BD28Xht12rsb%2FL, PID: 16959325
    • Frid P, Anisimov SV, Popovic N (2007) Congo red and protein aggregation in neurodegenerative diseases. Brain Res Rev 53:135–160. doi:10.1016/j.brainresrev.2006.08.001
    • (2007) Brain Res Rev , vol.53 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 145
    • 84881539841 scopus 로고    scopus 로고
    • 3D NMR structure of a complex between the amyloid beta peptide (1–40) and the polyphenol ε-viniferin glucoside: implications in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC3sXhsV2mu7zM, PID: 23830862
    • Richard T, Papastamoulis Y, Waffo-Teguo P, Monti JP (2013) 3D NMR structure of a complex between the amyloid beta peptide (1–40) and the polyphenol ε-viniferin glucoside: implications in Alzheimer’s disease. Biochim Biophys Acta 1830:5068–5074. doi:10.1016/j.bbagen.2013.06.031
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 5068-5074
    • Richard, T.1    Papastamoulis, Y.2    Waffo-Teguo, P.3    Monti, J.P.4
  • 146
    • 77951892516 scopus 로고    scopus 로고
    • Bioavailability of the polyphenols: status and controversies
    • PID: 20480022
    • D’Archivio M, Filesi C, Varì R, Scazzocchio B, Masella R (2010) Bioavailability of the polyphenols: status and controversies. Int J Mol Sci 11:1321–1342. doi:10.3390/ijms11041321
    • (2010) Int J Mol Sci , vol.11 , pp. 1321-1342
    • D’Archivio, M.1    Filesi, C.2    Varì, R.3    Scazzocchio, B.4    Masella, R.5


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