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Volumn 361, Issue , 2016, Pages 256-271

Alzheimer's disease: An overview of amyloid beta dependent pathogenesis and its therapeutic implications along with in silico approaches emphasizing the role of natural products

Author keywords

3D QSAR; Alzheimer's disease; Amyloid beta; Molecular docking and dynamics simulation; Resveratrol; Terpenoids

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR ANTAGONIST; ALPHA SECRETASE; AMYLOID BETA PROTEIN; ANTIINFLAMMATORY AGENT; BETA SECRETASE INHIBITOR; CHOLESTEROL; GAMMA SECRETASE INHIBITOR; NATURAL PRODUCT; VACCINE;

EID: 84959010623     PISSN: 0022510X     EISSN: 18785883     Source Type: Journal    
DOI: 10.1016/j.jns.2016.01.008     Document Type: Review
Times cited : (118)

References (170)
  • 4
    • 34248210710 scopus 로고    scopus 로고
    • A natural scavenger of peroxynitrites, rosmarinic acid, protects against impairment of memory induced by Abeta (25-35)
    • T. Alkam, A. Nitta, H. Mizoguchi, A. Itoh, and T. Nabeshima A natural scavenger of peroxynitrites, rosmarinic acid, protects against impairment of memory induced by Abeta (25-35) Behav. Brain Res. 180 2007 139 145
    • (2007) Behav. Brain Res. , vol.180 , pp. 139-145
    • Alkam, T.1    Nitta, A.2    Mizoguchi, H.3    Itoh, A.4    Nabeshima, T.5
  • 5
    • 84919395068 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association
    • Alzheimer's Association Alzheimer's disease facts and figures Alzheimers Dement. 10 2014 (http://www.alz.org/downloads/Facts-Figures-2014.pdf)
    • (2014) Alzheimers Dement. , vol.10
  • 6
    • 84886600387 scopus 로고    scopus 로고
    • Therapeutics of Alzheimer's disease: Past, present and future
    • R. Anand, K.D. Gill, and A.A. Mahdi Therapeutics of Alzheimer's disease: past, present and future Neuropharmacology 76 2014 27 50
    • (2014) Neuropharmacology , vol.76 , pp. 27-50
    • Anand, R.1    Gill, K.D.2    Mahdi, A.A.3
  • 7
    • 61749103704 scopus 로고    scopus 로고
    • Protective effect of quercetin in primary neurons against Abeta (1-42): Relevance to Alzheimer's disease
    • M.A. Ansari, H.M. Abdul, G. Joshi, W.O. Opii, and D.A. Butterfield Protective effect of quercetin in primary neurons against Abeta (1-42): relevance to Alzheimer's disease J. Nutr. Biochem. 20 2009 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
  • 8
    • 77951622086 scopus 로고    scopus 로고
    • In vitro antioxidant activities and an investigation of neuroprotection by six Salvia species from Iran: A comparative study
    • S. Asadi, A. Ahmadiani, M.A. Esmaeili, A. Sonboli, N. Ansari, and F. Khodagholi In vitro antioxidant activities and an investigation of neuroprotection by six Salvia species from Iran: a comparative study Food Chem. Toxicol. 48 2010 1341 1349
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 1341-1349
    • Asadi, S.1    Ahmadiani, A.2    Esmaeili, M.A.3    Sonboli, A.4    Ansari, N.5    Khodagholi, F.6
  • 16
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers: What you see is not always what you get
    • G. Bitan, E.A. Fradinger, S.M. Spring, and D.B. Teplow Neurotoxic protein oligomers: what you see is not always what you get Amyloid 12 2005 88 95
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 17
    • 0141738373 scopus 로고    scopus 로고
    • CSF markers for incipient Alzheimer's disease
    • K. Blennow, and H. Hampel CSF markers for incipient Alzheimer's disease Lancet Neurol. 2 2003 605 613
    • (2003) Lancet Neurol. , vol.2 , pp. 605-613
    • Blennow, K.1    Hampel, H.2
  • 18
    • 84991267536 scopus 로고    scopus 로고
    • Treatment of Alzheimer disease using combination therapy with plasma exchange and haemapheresis with albumin and intravenous immunoglobulin: Rationale and treatment approach of the AMBAR (Alzheimer Management by Albumin Replacement) study
    • M. Boada, E. Ramos-Fernández, B. Guivernau, F.J. Muñoz, M. Costa, A.M. Ortiz, J.I. Jorquera, L. Núñez, M. Torres, and A. Páez Treatment of Alzheimer disease using combination therapy with plasma exchange and haemapheresis with albumin and intravenous immunoglobulin: rationale and treatment approach of the AMBAR (Alzheimer Management by Albumin Replacement) study Neurologia 9 2014 30 39
    • (2014) Neurologia , vol.9 , pp. 30-39
    • Boada, M.1    Ramos-Fernández, E.2    Guivernau, B.3    Muñoz, F.J.4    Costa, M.5    Ortiz, A.M.6    Jorquera, J.I.7    Núñez, L.8    Torres, M.9    Páez, A.10
  • 21
  • 22
    • 33745661717 scopus 로고    scopus 로고
    • Efficacy and safety of memantine in moderate-to-severe Alzheimer disease: The evidence to date
    • R. Bullock Efficacy and safety of memantine in moderate-to-severe Alzheimer disease: the evidence to date Alzheimer Dis. Assoc. Disord. 20 2006 23 29
    • (2006) Alzheimer Dis. Assoc. Disord. , vol.20 , pp. 23-29
    • Bullock, R.1
  • 23
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Abeta1-42, in differentiated PC12 cells
    • D. Burdick, J. Kosmoski, M.F. Knauer, and C.G. Glabe Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Abeta1-42, in differentiated PC12 cells Brain Res. 746 1997 275 284
    • (1997) Brain Res. , vol.746 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 24
    • 84872970450 scopus 로고    scopus 로고
    • Safety and pharmacology of ponezumab (PF-04360365) after a single 10-minute intravenous infusion in subjects with mild to moderate Alzheimer disease
    • A.H. Burstein, Q. Zhao, J. Ross, S. Styren, J.W. Landen, W.W. Ma, F. McCush, C. Alvey, J.W. Kupiec, and M.M. Bednar Safety and pharmacology of ponezumab (PF-04360365) after a single 10-minute intravenous infusion in subjects with mild to moderate Alzheimer disease Clin. Neuropharmacol. 36 2013 8 13
    • (2013) Clin. Neuropharmacol. , vol.36 , pp. 8-13
    • Burstein, A.H.1    Zhao, Q.2    Ross, J.3    Styren, S.4    Landen, J.W.5    Ma, W.W.6    McCush, F.7    Alvey, C.8    Kupiec, J.W.9    Bednar, M.M.10
  • 27
    • 84856831983 scopus 로고    scopus 로고
    • Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic Drosophila
    • I. Caesar, M. Jonson, K.P. Nilsson, S. Thor, and P. Hammarström Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic Drosophila PLoS One 7 2012 314 324
    • (2012) PLoS One , vol.7 , pp. 314-324
    • Caesar, I.1    Jonson, M.2    Nilsson, K.P.3    Thor, S.4    Hammarström, P.5
  • 29
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • M. Calamai, F. Chiti, and C.M. Dobson Amyloid fibril formation can proceed from different conformations of a partially unfolded protein Biophys. J. 89 2005 4201 4210
    • (2005) Biophys. J. , vol.89 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 32
    • 79251490138 scopus 로고    scopus 로고
    • Current perspectives on pharmacotherapy of Alzheimer's disease
    • K. Chopra, S. Misra, and A. Kuhad Current perspectives on pharmacotherapy of Alzheimer's disease Expert. Opin. Pharmacother. 12 2011 335 350
    • (2011) Expert. Opin. Pharmacother. , vol.12 , pp. 335-350
    • Chopra, K.1    Misra, S.2    Kuhad, A.3
  • 34
    • 0030817292 scopus 로고    scopus 로고
    • Effects of beta-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: Evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor
    • R.F. Cowburn, B. Wiehager, E. Trief, M. Li-Li, and E. Sundstrom Effects of beta-amyloid-(25-35) peptides on radioligand binding to excitatory amino acid receptors and voltage-dependent calcium channels: evidence for a selective affinity for the glutamate and glycine recognition sites of the NMDA receptor Neurochem. Res. 22 1997 1437 1442
    • (1997) Neurochem. Res. , vol.22 , pp. 1437-1442
    • Cowburn, R.F.1    Wiehager, B.2    Trief, E.3    Li-Li, M.4    Sundstrom, E.5
  • 37
    • 77950941375 scopus 로고    scopus 로고
    • Amyloid-beta fibrillogenesis: Structural insight and therapeutic intervention
    • K.A. DaSilva, J.E. Shaw, and J. McLAurin Amyloid-beta fibrillogenesis: structural insight and therapeutic intervention Exp. Neurol. 223 2010 311 321
    • (2010) Exp. Neurol. , vol.223 , pp. 311-321
    • DaSilva, K.A.1    Shaw, J.E.2    McLAurin, J.3
  • 41
    • 77953497252 scopus 로고    scopus 로고
    • Clinical trials of EHT0202, a neuroprotective and procognitive alpha-secretase
    • L. Desire, M. Marcade, H. Peillon, D. Drouin, and O. Sol Clinical trials of EHT0202, a neuroprotective and procognitive alpha-secretase Alzheimers Dement. 5 2009 255 256
    • (2009) Alzheimers Dement. , vol.5 , pp. 255-256
    • Desire, L.1    Marcade, M.2    Peillon, H.3    Drouin, D.4    Sol, O.5
  • 43
    • 84866744899 scopus 로고    scopus 로고
    • Berberine ameliorates β-amyloid pathology, gliosis, and cognitive impairment in an Alzheimer's disease transgenic mouse model
    • S.S. Durairajan, L.F. Liu, J.H. Lu, L.L. Chen, Q. Yuan, S.K. Chung, L. Huang, X.S. Li, J.D. Huang, and M. Li Berberine ameliorates β-amyloid pathology, gliosis, and cognitive impairment in an Alzheimer's disease transgenic mouse model Neurobiol. Aging 33 2012 2903 2919
    • (2012) Neurobiol. Aging , vol.33 , pp. 2903-2919
    • Durairajan, S.S.1    Liu, L.F.2    Lu, J.H.3    Chen, L.L.4    Yuan, Q.5    Chung, S.K.6    Huang, L.7    Li, X.S.8    Huang, J.D.9    Li, M.10
  • 50
    • 84870057502 scopus 로고    scopus 로고
    • The binding of resveratrol to monomer and fibril amyloid beta
    • J.F. Ge, J.P. Qiao, C.C. Qi, C.W. Wang, and J.N. Zhou The binding of resveratrol to monomer and fibril amyloid beta Neurochem. Int. 61 2012 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
  • 51
    • 78651322583 scopus 로고    scopus 로고
    • A randomized pilot clinical trial of the safety of pioglitazone in treatment of patients with Alzheimer disease
    • D.S. Geldmacher, T. Fritsch, M.J. McClendon, and G. Landreth A randomized pilot clinical trial of the safety of pioglitazone in treatment of patients with Alzheimer disease Arch. Neurol. 68 2011 45 50
    • (2011) Arch. Neurol. , vol.68 , pp. 45-50
    • Geldmacher, D.S.1    Fritsch, T.2    McClendon, M.J.3    Landreth, G.4
  • 52
    • 72549105935 scopus 로고    scopus 로고
    • Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: A randomized controlled trial
    • R.C. Green, L.S. Schneider, D.A. Amato, A.P. Beelen, G. Wilcock, E.A. Swabb, and K.H. Zavitz Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial J. Am. Med. Assoc. 302 2009 2557 2564
    • (2009) J. Am. Med. Assoc. , vol.302 , pp. 2557-2564
    • Green, R.C.1    Schneider, L.S.2    Amato, D.A.3    Beelen, A.P.4    Wilcock, G.5    Swabb, E.A.6    Zavitz, K.H.7
  • 54
    • 0035142278 scopus 로고    scopus 로고
    • Cholinesterase inhibitors for Alzheimer's disease
    • J. Grutzendler, and J.C. Morris Cholinesterase inhibitors for Alzheimer's disease Drugs 61 2001 41 52
    • (2001) Drugs , vol.61 , pp. 41-52
    • Grutzendler, J.1    Morris, J.C.2
  • 55
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer's disease-proteolysis holds the key
    • C. Haass, and B. De Strooper The presenilins in Alzheimer's disease-proteolysis holds the key Science 286 1999 916 919
    • (1999) Science , vol.286 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 56
    • 0026325645 scopus 로고
    • Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion
    • C. Haass, A.Y. Hung, and D.J. Selkoe Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion J. Neurosci. 11 1991 3783 3793
    • (1991) J. Neurosci. , vol.11 , pp. 3783-3793
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3
  • 59
    • 84925231908 scopus 로고    scopus 로고
    • Primary prevention of Alzheimer's disease: Is it an attainable goal?
    • J.Y. Han, and S.H. Han Primary prevention of Alzheimer's disease: is it an attainable goal? J. Korean Med. Sci. 29 2014 886 892
    • (2014) J. Korean Med. Sci. , vol.29 , pp. 886-892
    • Han, J.Y.1    Han, S.H.2
  • 60
    • 0032150877 scopus 로고    scopus 로고
    • Genetic dissection of Alzheimer's disease and related dementias: Amyloid and its relationship to tau
    • J. Hardy, K. Duff, K. Hardy, J. Perez-Tur, and M. Hutton Genetic dissection of Alzheimer's disease and related dementias: amyloid and its relationship to tau Nat. Neurosci. 1 1998 355 358
    • (1998) Nat. Neurosci. , vol.1 , pp. 355-358
    • Hardy, J.1    Duff, K.2    Hardy, K.3    Perez-Tur, J.4    Hutton, M.5
  • 61
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 62
    • 67650407720 scopus 로고    scopus 로고
    • Development of semagacestat (LY450139), a functional γ-secretase inhibitor, for the treatment of Alzheimer's disease
    • D.B. Henley, P.C. May, R.A. Dean, and E.R. Siemers Development of semagacestat (LY450139), a functional γ-secretase inhibitor, for the treatment of Alzheimer's disease Expert. Opin. Pharmacother. 10 2009 1657 1664
    • (2009) Expert. Opin. Pharmacother. , vol.10 , pp. 1657-1664
    • Henley, D.B.1    May, P.C.2    Dean, R.A.3    Siemers, E.R.4
  • 63
    • 0033569444 scopus 로고    scopus 로고
    • Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation
    • D.R. Howlett, A.R. George, D.E. Owen, R.V. Ward, and R.E. Markwell Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation Biochem. J. 343 1999 419 423
    • (1999) Biochem. J. , vol.343 , pp. 419-423
    • Howlett, D.R.1    George, A.R.2    Owen, D.E.3    Ward, R.V.4    Markwell, R.E.5
  • 65
    • 40349111175 scopus 로고    scopus 로고
    • Therapeutic potential of γ-secretase inhibitors and modulators
    • B. Imbimbo Therapeutic potential of γ-secretase inhibitors and modulators Curr. Top. Med. Chem. 8 2008 54 61
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 54-61
    • Imbimbo, B.1
  • 66
    • 68049148021 scopus 로고    scopus 로고
    • Why did tarenflurbil fail in Alzheimer's disease?
    • B.P. Imbimbo Why did tarenflurbil fail in Alzheimer's disease? J. Alzheimers Dis. 17 2009 757 760
    • (2009) J. Alzheimers Dis. , vol.17 , pp. 757-760
    • Imbimbo, B.P.1
  • 68
    • 0037088914 scopus 로고    scopus 로고
    • Microglial activation and beta-amyloid deposit reduction caused by a nitric oxide-releasing nonsteroidal anti-inflammatory drug in amyloid precursor protein plus presenilin-1 transgenic mice
    • P.T. Jantzen, K.E. Connor, G. DiCarlo, G.L. Wenk, J.L. Wallace, A.M. Rojiani, D. Coppola, D. Morgan, and M.N. Gordon Microglial activation and beta-amyloid deposit reduction caused by a nitric oxide-releasing nonsteroidal anti-inflammatory drug in amyloid precursor protein plus presenilin-1 transgenic mice J. Neurosci. 22 2002 2246 2254
    • (2002) J. Neurosci. , vol.22 , pp. 2246-2254
    • Jantzen, P.T.1    Connor, K.E.2    DiCarlo, G.3    Wenk, G.L.4    Wallace, J.L.5    Rojiani, A.M.6    Coppola, D.7    Morgan, D.8    Gordon, M.N.9
  • 69
    • 84929051777 scopus 로고    scopus 로고
    • Potential therapeutic strategies for Alzheimer's disease targeting or beyond β-amyloid: Insights from clinical trials
    • Q. Jia, Y. Deng, and H. Qing Potential therapeutic strategies for Alzheimer's disease targeting or beyond β-amyloid: insights from clinical trials Biomed Res. Int. 2014 22
    • (2014) Biomed Res. Int. , pp. 22
    • Jia, Q.1    Deng, Y.2    Qing, H.3
  • 70
    • 84855730408 scopus 로고    scopus 로고
    • Quercetin and rutin exhibit anti amyloidogenic and fibril disaggregating effects in vitro and potent antioxidant activity in APPswe cells
    • K. Jiménez-Aliaga, P. Bermejo-Bescós, J. Benedí, and S. Martín-Aragón Quercetin and rutin exhibit anti amyloidogenic and fibril disaggregating effects in vitro and potent antioxidant activity in APPswe cells Life Sci. 89 2011 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
  • 72
    • 77949655624 scopus 로고    scopus 로고
    • Chitosan prevents oxidative stress-induced amyloid beta formation and cytotoxicity in NT2 neurons: Involvement of transcription factors Nrf2 and NF-kappaB
    • F. Khodagholi, B. Eftekharzadeh, N. Maghsoudi, and P.F. Rezaei Chitosan prevents oxidative stress-induced amyloid beta formation and cytotoxicity in NT2 neurons: involvement of transcription factors Nrf2 and NF-kappaB Mol. Cell. Biochem. 337 2010 39 51
    • (2010) Mol. Cell. Biochem. , vol.337 , pp. 39-51
    • Khodagholi, F.1    Eftekharzadeh, B.2    Maghsoudi, N.3    Rezaei, P.F.4
  • 75
    • 16644371785 scopus 로고    scopus 로고
    • The beta-amyloid cascade hypothesis: A sequence of events leading to neurodegeneration in Alzheimer's disease
    • A. Kowalska The beta-amyloid cascade hypothesis: a sequence of events leading to neurodegeneration in Alzheimer's disease Neurol. Neurochir. Pol. 38 2004 405 411
    • (2004) Neurol. Neurochir. Pol. , vol.38 , pp. 405-411
    • Kowalska, A.1
  • 76
    • 79251550418 scopus 로고    scopus 로고
    • Mechanisms of amyloid-beta peptide uptake by neurons: The role of lipid rafts and lipid raft-associated proteins
    • A.Y. Lai, and J. McLaurin Mechanisms of amyloid-beta peptide uptake by neurons: the role of lipid rafts and lipid raft-associated proteins Int. J. Alzheimers Dis. 2011 2010 548380
    • (2010) Int. J. Alzheimers Dis. , vol.2011 , pp. 548380
    • Lai, A.Y.1    McLaurin, J.2
  • 77
    • 84876749121 scopus 로고    scopus 로고
    • First-in-human study of E2609, a novel BACE1 inhibitor, demonstrates prolonged reductions in plasma beta-amyloid levels after single dosing
    • R. Lai, B. Albala, J.M. Kaplow, J. Aluri, M. Yen, and A. Satlin First-in-human study of E2609, a novel BACE1 inhibitor, demonstrates prolonged reductions in plasma beta-amyloid levels after single dosing Alzheimers Dement. 8 2012 96
    • (2012) Alzheimers Dement. , vol.8 , pp. 96
    • Lai, R.1    Albala, B.2    Kaplow, J.M.3    Aluri, J.4    Yen, M.5    Satlin, A.6
  • 78
    • 84872960603 scopus 로고    scopus 로고
    • Safety and pharmacology of a single intravenous dose of ponezumab in subjects with mild-to-moderate Alzheimer disease: A phase I, randomized, placebo-controlled, double-blind, dose-escalation study
    • J.W. Landen, Q. Zhao, S. Cohen, M. Borrie, M. Woodward, C.B. Billing Jr., K. Bales, C. Alvey, F. McCush, J. Yang, J.W. Kupiec, and M.M. Bednar Safety and pharmacology of a single intravenous dose of ponezumab in subjects with mild-to-moderate Alzheimer disease: a phase I, randomized, placebo-controlled, double-blind, dose-escalation study Clin. Neuropharmacol. 36 2013 14 23
    • (2013) Clin. Neuropharmacol. , vol.36 , pp. 14-23
    • Landen, J.W.1    Zhao, Q.2    Cohen, S.3    Borrie, M.4    Woodward, M.5    Billing, C.B.6    Bales, K.7    Alvey, C.8    McCush, F.9    Yang, J.10    Kupiec, J.W.11    Bednar, M.M.12
  • 79
    • 46749115113 scopus 로고    scopus 로고
    • PPAR gamma agonists as therapeutics for the treatment of Alzheimer's disease
    • G. Landreth, Q. Jiang, S. Mandrekar, and M. Heneka PPAR gamma agonists as therapeutics for the treatment of Alzheimer's disease Neurotherapeutics 5 2008 481 489
    • (2008) Neurotherapeutics , vol.5 , pp. 481-489
    • Landreth, G.1    Jiang, Q.2    Mandrekar, S.3    Heneka, M.4
  • 81
    • 84989182917 scopus 로고    scopus 로고
    • Perspectives on future Alzheimer therapies: Amyloid-β protofibrils-A new target for immunotherapy with BAN2401 in Alzheimer's disease
    • L. Lannfelt, C. Möller, H. Basun, G. Osswald, D. Sehlin, A. Satlin, V. Logovinsky, and P. Gellerfors Perspectives on future Alzheimer therapies: amyloid-β protofibrils-a new target for immunotherapy with BAN2401 in Alzheimer's disease Alzheimers Res. Ther. 6 2014 16
    • (2014) Alzheimers Res. Ther. , vol.6 , pp. 16
    • Lannfelt, L.1    Möller, C.2    Basun, H.3    Osswald, G.4    Sehlin, D.5    Satlin, A.6    Logovinsky, V.7    Gellerfors, P.8
  • 82
    • 84870456663 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate prevents systemic inflammation-induced memory deficiency and amyloidogenesis via its antineuroinflammatory properties
    • Y.J. Lee, D.Y. Choi, Y.P. Yun, S.B. Han, K.W. Oh, and J.T. Hong Epigallocatechin-3-gallate prevents systemic inflammation-induced memory deficiency and amyloidogenesis via its antineuroinflammatory properties J. Nutr. Biochem. 24 2012 298 310
    • (2012) J. Nutr. Biochem. , vol.24 , pp. 298-310
    • Lee, Y.J.1    Choi, D.Y.2    Yun, Y.P.3    Han, S.B.4    Oh, K.W.5    Hong, J.T.6
  • 83
    • 84886937126 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease: Hoops and hurdles
    • C.A. Lemere Immunotherapy for Alzheimer's disease: hoops and hurdles Mol. Neurodegener. 8 2013 36
    • (2013) Mol. Neurodegener. , vol.8 , pp. 36
    • Lemere, C.A.1
  • 85
    • 84855853383 scopus 로고    scopus 로고
    • Resveratrol, a neuroprotective supplement for Alzheimer's disease
    • F. Li, Q. Gong, H. Dong, and J. Shi Resveratrol, a neuroprotective supplement for Alzheimer's disease Curr. Pharm. Des. 18 2012 27 33
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 27-33
    • Li, F.1    Gong, Q.2    Dong, H.3    Shi, J.4
  • 86
    • 10644230076 scopus 로고    scopus 로고
    • (-)-Epigallocatechin gallate inhibits lipopolysaccharide-induced microglial activation and protects against inflammation-mediated dopaminergic neuronal injury
    • R. Li, Y.G. Huang, D. Fang, and W.D. Le (-)-Epigallocatechin gallate inhibits lipopolysaccharide-induced microglial activation and protects against inflammation-mediated dopaminergic neuronal injury J. Neurosci. Res. 78 2004 723 731
    • (2004) J. Neurosci. Res. , vol.78 , pp. 723-731
    • Li, R.1    Huang, Y.G.2    Fang, D.3    Le, W.D.4
  • 87
    • 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
    • R. Liu, F. Meng, L. Zhang, A. Liu, H. Qin, X. Lan, L. Li, and G. Du 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 16 2011 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
  • 88
    • 31144450053 scopus 로고    scopus 로고
    • Current pharmacotherapy for Alzheimer's disease
    • A. Lleo, S.M. Greenberg, and J.H. Growdon Current pharmacotherapy for Alzheimer's disease Annu. Rev. Med. 57 2006 513 533
    • (2006) Annu. Rev. Med. , vol.57 , pp. 513-533
    • Lleo, A.1    Greenberg, S.M.2    Growdon, J.H.3
  • 93
    • 54249143535 scopus 로고    scopus 로고
    • Cell signaling pathways and iron chelation in the neurorestorative activity of green tea polyphenols: Special reference to epigallocatechin gallate (EGCG)
    • S.A. Mandel, T. Amit, L. Kalfon, L. Reznichenko, O. Weinreb, and M.B.H. Youdim Cell signaling pathways and iron chelation in the neurorestorative activity of green tea polyphenols: special reference to epigallocatechin gallate (EGCG) J. Alzheimers Dis. 15 2008 211 222
    • (2008) J. Alzheimers Dis. , vol.15 , pp. 211-222
    • Mandel, S.A.1    Amit, T.2    Kalfon, L.3    Reznichenko, L.4    Weinreb, O.5    Youdim, M.B.H.6
  • 99
    • 68149179573 scopus 로고    scopus 로고
    • Immuno-senescence: What does it mean to health outcomes in older adults?
    • J.E. McElhaney, and R.B. Effros Immuno-senescence: what does it mean to health outcomes in older adults? Curr. Opin. Immunol. 21 2009 418 424
    • (2009) Curr. Opin. Immunol. , vol.21 , pp. 418-424
    • McElhaney, J.E.1    Effros, R.B.2
  • 101
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit Abeta-induced toxicity
    • J. McLaurin, R. Golomb, A. Jurewicz, J.P. Antel, and P.E. Fraser Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit Abeta-induced toxicity J. Biol. Chem. 275 2000 18495 18502
    • (2000) J. Biol. Chem. , vol.275 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 102
    • 0035907123 scopus 로고    scopus 로고
    • Amyloid beta protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease
    • P.D. Mehta, T. Pirttila, B.A. Patrick, M. Barshatzky, and S.P. Mehta Amyloid beta protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease Neurosci. Lett. 304 2001 102 106
    • (2001) Neurosci. Lett. , vol.304 , pp. 102-106
    • Mehta, P.D.1    Pirttila, T.2    Patrick, B.A.3    Barshatzky, M.4    Mehta, S.P.5
  • 103
    • 84865077476 scopus 로고    scopus 로고
    • Stopping Alzheimer's before it starts
    • G. Miller Stopping Alzheimer's before it starts Science 337 2012 790 792
    • (2012) Science , vol.337 , pp. 790-792
    • Miller, G.1
  • 106
    • 84877254025 scopus 로고    scopus 로고
    • Passive anti-amyloid immunotherapy in Alzheimer's disease: What are the most promising targets?
    • J. Moreth, C. Mavoungou, and K. Schindowski Passive anti-amyloid immunotherapy in Alzheimer's disease: what are the most promising targets? Immun. Ageing 10 2013 18
    • (2013) Immun. Ageing , vol.10 , pp. 18
    • Moreth, J.1    Mavoungou, C.2    Schindowski, K.3
  • 107
    • 84924340811 scopus 로고    scopus 로고
    • Anti-cholinergic alkaloids as potential therapeutic agents for Alzheimer's disease: An in silico approach
    • H. Naaz, S. Singh, V.P. Pandey, P. Singh, and U.N. Dwivedi Anti-cholinergic alkaloids as potential therapeutic agents for Alzheimer's disease: an in silico approach Ind. J. Biochem. Biophys. 50 2013 120 125
    • (2013) Ind. J. Biochem. Biophys. , vol.50 , pp. 120-125
    • Naaz, H.1    Singh, S.2    Pandey, V.P.3    Singh, P.4    Dwivedi, U.N.5
  • 109
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from 1981 to 2010
    • D.J. Newman, and G.M. Cragg Natural products as sources of new drugs over the 30 years from 1981 to 2010 J. Nat. Prod. 75 2012 311 335
    • (2012) J. Nat. Prod. , vol.75 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 111
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • S. Oddo, L. Billings, J.P. Kesslak, D.H. Cribbs, and F.M. LaFerla Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome Neuron 43 2004 321 332
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 123
    • 33847006236 scopus 로고    scopus 로고
    • Effect of statins on Alzheimer's disease biomarkers in cerebrospinal fluid
    • R.G. Riekse, G. Li, E.C. Petrie, and et al. Effect of statins on Alzheimer's disease biomarkers in cerebrospinal fluid J. Alzheimers Dis. 10 2006 399 406
    • (2006) J. Alzheimers Dis. , vol.10 , pp. 399-406
    • Riekse, R.G.1    Li, G.2    Petrie, E.C.3
  • 126
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue
    • A.E. Roher, K.C. Palmer, E.C. Yurewicz, M.J. Ball, and B.D. Greenberg Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue J. Neurochem. 61 1993 1916 1926
    • (1993) J. Neurochem. , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Yurewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 127
    • 67849102202 scopus 로고    scopus 로고
    • Anti-amyloid-beta immunotherapy in Alzheimer's disease: ACC-001 clinical trials are ongoing
    • J.M. Ryan, and M. Grundman Anti-amyloid-beta immunotherapy in Alzheimer's disease: ACC-001 clinical trials are ongoing J. Alzheimers Dis. 17 2009 243
    • (2009) J. Alzheimers Dis. , vol.17 , pp. 243
    • Ryan, J.M.1    Grundman, M.2
  • 128
    • 80052258842 scopus 로고    scopus 로고
    • PF-04494700, an oral inhibitor of receptor for advanced glycation end products (RAGE), in Alzheimer disease
    • M.N. Sabbagh, A. Agro, J. Bell, P.S. Aisen, E. Schweizer, and D. Galasko PF-04494700, an oral inhibitor of receptor for advanced glycation end products (RAGE), in Alzheimer disease Alzheimer Dis. Assoc. Disord. 25 2011 206 212
    • (2011) Alzheimer Dis. Assoc. Disord. , vol.25 , pp. 206-212
    • Sabbagh, M.N.1    Agro, A.2    Bell, J.3    Aisen, P.S.4    Schweizer, E.5    Galasko, D.6
  • 129
    • 84940996844 scopus 로고    scopus 로고
    • Computational approaches for drug design and discovery process
    • B.M. Sahoo, S.C. Dinda, R. Kumar, and J.R. Panda Computational approaches for drug design and discovery process Curr. Pharma Res. 2 2012 600 611
    • (2012) Curr. Pharma Res. , vol.2 , pp. 600-611
    • Sahoo, B.M.1    Dinda, S.C.2    Kumar, R.3    Panda, J.R.4
  • 132
    • 84895523900 scopus 로고    scopus 로고
    • The pathogenic Aβ43 is enriched in familial and sporadic Alzheimer disease
    • A. Sandebring, H. Welander, B. Winblad, C. Graff, and L.O. Tjernberg The pathogenic Aβ43 is enriched in familial and sporadic Alzheimer disease PLoS One 8 2013 e55847
    • (2013) PLoS One , vol.8 , pp. e55847
    • Sandebring, A.1    Welander, H.2    Winblad, B.3    Graff, C.4    Tjernberg, L.O.5
  • 133
    • 84856454638 scopus 로고    scopus 로고
    • A novel multivalent Abeta peptide vaccine with preclinical evidence of a central immune response that generates antisera recognizing a wide range of abeta peptide species
    • M.J. Savage, G. Wu, A. McCampbell, K.R. Wessner, M. Citron, X. Liang, S. Hsieh, A.L. Wolfe, G.G. Kinney, L.B. Rosen, and J.J. Renger A novel multivalent Abeta peptide vaccine with preclinical evidence of a central immune response that generates antisera recognizing a wide range of abeta peptide species Alzheimers Dement. 6 2010 142
    • (2010) Alzheimers Dement. , vol.6 , pp. 142
    • Savage, M.J.1    Wu, G.2    McCampbell, A.3    Wessner, K.R.4    Citron, M.5    Liang, X.6    Hsieh, S.7    Wolfe, A.L.8    Kinney, G.G.9    Rosen, L.B.10    Renger, J.J.11
  • 135
    • 0034695098 scopus 로고    scopus 로고
    • The biology of the receptor for advanced glycation end products and its ligands
    • A. Schmidt, S. Yan, S. Yan, and D. Stern The biology of the receptor for advanced glycation end products and its ligands Biochim. Biophys. Acta 1498 2000 99 111
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 99-111
    • Schmidt, A.1    Yan, S.2    Yan, S.3    Stern, D.4
  • 136
  • 137
    • 84856393256 scopus 로고    scopus 로고
    • The phosphatidyl inositol 3 kinase-glycogen synthase kinase 3β pathway mediates bilobalide-induced reduction in amyloid β-peptide
    • C. Shi, D.D. Zheng, F.M. Wu, J. Liu, and J. Xu The phosphatidyl inositol 3 kinase-glycogen synthase kinase 3β pathway mediates bilobalide-induced reduction in amyloid β-peptide Neurochem. Res. 37 2012 298 306
    • (2012) Neurochem. Res. , vol.37 , pp. 298-306
    • Shi, C.1    Zheng, D.D.2    Wu, F.M.3    Liu, J.4    Xu, J.5
  • 139
    • 84890517097 scopus 로고    scopus 로고
    • Dementia (including Alzheimer's disease) can be prevented: Statement supported by international experts
    • A.D. Smith, and K. Yaffe Dementia (including Alzheimer's disease) can be prevented: statement supported by international experts J. Alzheimers Dis. 38 2014 699 703
    • (2014) J. Alzheimers Dis. , vol.38 , pp. 699-703
    • Smith, A.D.1    Yaffe, K.2
  • 140
    • 0034098980 scopus 로고    scopus 로고
    • Alterations of Alzheimer's disease in the cholesterol-fed rabbit, including vascular inflammation. Preliminary observations
    • D.L. Sparks, Y.M. Kuo, A. Roher, T. Martin, and R.J. Lukas Alterations of Alzheimer's disease in the cholesterol-fed rabbit, including vascular inflammation. Preliminary observations Ann. N. Y. Acad. Sci. 903 2000 335 344
    • (2000) Ann. N. Y. Acad. Sci. , vol.903 , pp. 335-344
    • Sparks, D.L.1    Kuo, Y.M.2    Roher, A.3    Martin, T.4    Lukas, R.J.5
  • 143
    • 48449084725 scopus 로고    scopus 로고
    • Synthesis of scyllo-inositol derivatives and their effects on amyloid beta peptide aggregation
    • Y. Sun, G. Zhang, C.A. Hawkes, J.E. Shaw, J. McLaurin, and M. Nitz Synthesis of scyllo-inositol derivatives and their effects on amyloid beta peptide aggregation Bioorg. Med. Chem. 16 2008 7177 7184
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7177-7184
    • Sun, Y.1    Zhang, G.2    Hawkes, C.A.3    Shaw, J.E.4    McLaurin, J.5    Nitz, M.6
  • 144
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • M. Sunde, and C.C.F. Blake The structure of amyloid fibrils by electron microscopy and X-ray diffraction Adv. Protein Chem. 50 1997 123 159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 145
    • 78049506839 scopus 로고    scopus 로고
    • Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits
    • R. Tamayev, S. Matsuda, M. Fa, O. Arancio, and L. D'Adamio Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits Proc. Natl. Acad. Sci. U. S. A. 107 2010 20822 20827
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20822-20827
    • Tamayev, R.1    Matsuda, S.2    Fa, M.3    Arancio, O.4    D'Adamio, L.5
  • 146
    • 77953496330 scopus 로고    scopus 로고
    • Beta-secretase as target for amyloid-reduction therapy
    • J.J.N. Tang Beta-secretase as target for amyloid-reduction therapy Alzheimers Dement. 5 2009 74
    • (2009) Alzheimers Dement. , vol.5 , pp. 74
    • Tang, J.J.N.1
  • 147
    • 84864479942 scopus 로고    scopus 로고
    • Evaluation of effectiveness of herbal medication in cancer care: A review study
    • J. Tavakoli, S. Miar, M.M. Zadehzare, and H. Akbari Evaluation of effectiveness of herbal medication in cancer care: a review study Iran J. Cancer Prev. 5 2012 144 156
    • (2012) Iran J. Cancer Prev. , vol.5 , pp. 144-156
    • Tavakoli, J.1    Miar, S.2    Zadehzare, M.M.3    Akbari, H.4
  • 150
    • 44049102976 scopus 로고    scopus 로고
    • Current and future therapy in Alzheimer's disease
    • R.J. van Marum Current and future therapy in Alzheimer's disease Fundam. Clin. Pharmacol. 22 2008 265 274
    • (2008) Fundam. Clin. Pharmacol. , vol.22 , pp. 265-274
    • Van Marum, R.J.1
  • 151
    • 84928122845 scopus 로고    scopus 로고
    • BACE1 inhibitor drugs in clinical trials for Alzheimer's disease
    • R. Vassar BACE1 inhibitor drugs in clinical trials for Alzheimer's disease Alzheimers Res. Ther. 6 2014 89
    • (2014) Alzheimers Res. Ther. , vol.6 , pp. 89
    • Vassar, R.1
  • 152
    • 84881155541 scopus 로고    scopus 로고
    • Natural products derived from plants as a source of drugs
    • C. Veeresham Natural products derived from plants as a source of drugs J. Adv. Pharm. Technol. Res. 3 2012 200 201
    • (2012) J. Adv. Pharm. Technol. Res. , vol.3 , pp. 200-201
    • Veeresham, C.1
  • 154
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • D.M. Walsh, B.P. Tseng, R.E. Rydel, M.B. Podlisny, and D.J. Selkoe The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain Biochemistry 39 2000 10831 10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 155
    • 79952756491 scopus 로고    scopus 로고
    • Huperzine A activates Wnt/β-catenin signaling and enhances the nonamyloidogenic pathway in an Alzheimer transgenic mouse model
    • C.Y. Wang, W. Zheng, T. Wang, J.W. Xie, S.L. Wang, B.L. Zhao, W.P. Teng, and Z.Y. Wang Huperzine A activates Wnt/β-catenin signaling and enhances the nonamyloidogenic pathway in an Alzheimer transgenic mouse model Neuropsychopharmacology 36 2011 1073 1089
    • (2011) Neuropsychopharmacology , vol.36 , pp. 1073-1089
    • Wang, C.Y.1    Zheng, W.2    Wang, T.3    Xie, J.W.4    Wang, S.L.5    Zhao, B.L.6    Teng, W.P.7    Wang, Z.Y.8
  • 156
    • 44049106870 scopus 로고    scopus 로고
    • The developmentof NIC5-15, a natural anti-diabetic agent, in the treatment of Alzheimer's disease
    • J. Wang, L. Ho, and G.M. Passinetti The developmentof NIC5-15, a natural anti-diabetic agent, in the treatment of Alzheimer's disease Alzheimers Dement. 1 2005 62
    • (2005) Alzheimers Dement. , vol.1 , pp. 62
    • Wang, J.1    Ho, L.2    Passinetti, G.M.3
  • 158
    • 83155180349 scopus 로고    scopus 로고
    • Huperzine A alleviates synaptic deficits and modulates amyloidogenic and nonamyloidogenic pathways in APPswe/PS1dE9 transgenic mice
    • Y. Wang, X.C. Tang, and H.Y. Zhang Huperzine A alleviates synaptic deficits and modulates amyloidogenic and nonamyloidogenic pathways in APPswe/PS1dE9 transgenic mice J. Neurosci. Res. 90 2012 508 517
    • (2012) J. Neurosci. Res. , vol.90 , pp. 508-517
    • Wang, Y.1    Tang, X.C.2    Zhang, H.Y.3
  • 161
    • 58149375748 scopus 로고    scopus 로고
    • Anti-amyloid-beta immunotherapy in Alzheimer's disease: Relevance of transgenic mouse studies to clinical trials
    • D.M. Wilcock, and C.A. Colton Anti-amyloid-beta immunotherapy in Alzheimer's disease: relevance of transgenic mouse studies to clinical trials J. Alzheimers Dis. 15 2008 555 569
    • (2008) J. Alzheimers Dis. , vol.15 , pp. 555-569
    • Wilcock, D.M.1    Colton, C.A.2
  • 162
    • 67649363905 scopus 로고    scopus 로고
    • Amyloid reduction by amyloid-β vaccination also reduces mouse tau pathology and protects from neuron loss in two mouse models of Alzheimer's disease
    • D.M. Wilcock, N. Gharkholonarehe, W.E. VanNostrand, J. Davis, M.P. Vitek, and C.A. Colton Amyloid reduction by amyloid-β vaccination also reduces mouse tau pathology and protects from neuron loss in two mouse models of Alzheimer's disease J. Neurosci. 29 2009 7957 7965
    • (2009) J. Neurosci. , vol.29 , pp. 7957-7965
    • Wilcock, D.M.1    Gharkholonarehe, N.2    VanNostrand, W.E.3    Davis, J.4    Vitek, M.P.5    Colton, C.A.6
  • 164
    • 76849109048 scopus 로고    scopus 로고
    • Results of the first-in-man study with the active Aβ immunotherapy CAD106 in Alzheimer patients
    • B. Winblad, L. Minthon, and A. Floesser Results of the first-in-man study with the active Aβ immunotherapy CAD106 in Alzheimer patients Alzheimers Dement. 5 2009 113 114
    • (2009) Alzheimers Dement. , vol.5 , pp. 113-114
    • Winblad, B.1    Minthon, L.2    Floesser, A.3
  • 165
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • B. Wolozin, W. Kellman, P. Ruosseau, G.G. Celesia, and G. Siegel Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors Arch. Neurol. 57 2000 1439 1443
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 166
    • 83155181938 scopus 로고    scopus 로고
    • Curcumin mediates presenilin-1 activity to reduce β-amyloid production in a model of Alzheimer's disease
    • Z. Xiong, Z. Hongmei, S. Lu, and L. Yu Curcumin mediates presenilin-1 activity to reduce β-amyloid production in a model of Alzheimer's disease Pharmacol. Rep. 63 2011 1101 1108
    • (2011) Pharmacol. Rep. , vol.63 , pp. 1101-1108
    • Xiong, Z.1    Hongmei, Z.2    Lu, S.3    Yu, L.4
  • 167
    • 0041921071 scopus 로고    scopus 로고
    • Anti-inflammatory drug therapy alters β-amyloid processing and deposition in an animal model of Alzheimer's disease
    • Q. Yan, J. Zhang, H. Liu, S. Babu-Khan, R. Vassar, A.L. Biere, M. Citron, and G. Landreth Anti-inflammatory drug therapy alters β-amyloid processing and deposition in an animal model of Alzheimer's disease J. Neurosci. 20 2003 7504 7509
    • (2003) J. Neurosci. , vol.20 , pp. 7504-7509
    • Yan, Q.1    Zhang, J.2    Liu, H.3    Babu-Khan, S.4    Vassar, R.5    Biere, A.L.6    Citron, M.7    Landreth, G.8
  • 169
    • 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
    • L. Zhao, J.L. Wang, Y.R. Wang, and X.Z. Fa Apigenin attenuates copper-mediated β-amyloid neurotoxicity through antioxidation, mitochondrion protection and MAPK signal inactivation in an AD cell model Brain Res. 1492 2013 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
  • 170
    • 84874943989 scopus 로고    scopus 로고
    • Hepatoprotection of berberine against hydrogen peroxide-induced apoptosis by upregulation of sirtuin 1
    • X. Zhu, X. Guo, G. Mao, Z. Gao, H. Wang, Q. He, and D. Li Hepatoprotection of berberine against hydrogen peroxide-induced apoptosis by upregulation of sirtuin 1 Phytother. Res. 27 2013 417 421
    • (2013) Phytother. Res. , vol.27 , pp. 417-421
    • Zhu, X.1    Guo, X.2    Mao, G.3    Gao, Z.4    Wang, H.5    He, Q.6    Li, D.7


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