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Volumn 5, Issue , 2013, Pages 23-31

Curcumin: A natural substance with potential efficacy in Alzheimer's disease

Author keywords

Alzheimer's disease; Curcumin; Neuroprotection; amyloid

Indexed keywords

AMYLOID BETA PROTEIN; BIOPERINE; BLACK PEPPER EXTRACT; CURCUMIN; DONEPEZIL; GALANTAMINE; LONGVIDA; MEMANTINE; NONSTEROID ANTIINFLAMMATORY AGENT; RIVASTIGMINE; UNCLASSIFIED DRUG;

EID: 85015468275     PISSN: None     EISSN: 11791454     Source Type: Journal    
DOI: 10.2147/JEP.S26803     Document Type: Article
Times cited : (49)

References (166)
  • 1
    • 0029091572 scopus 로고
    • Amyloid β amyloidosis in Alzheimer's disease
    • Price DL, Sisodia SS, Gandy SE. Amyloid β amyloidosis in Alzheimer's disease. Curr Opin Neurol. 1995;8(4):268-274.
    • (1995) Curr Opin Neurol , vol.8 , Issue.4 , pp. 268-274
    • Price, D.L.1    Sisodia, S.S.2    Gandy, S.E.3
  • 3
    • 85015471869 scopus 로고    scopus 로고
    • [homepage on the Internet]. Alzheimer's Disease Facts and Figures. Available from: http://www.alz.org/alzheimers-disease-facts-and-figures.asp. Accessed April 8, 2013
    • www.alz.org [homepage on the Internet]. Alzheimer's Disease Facts and Figures. Available from: http://www.alz.org/alzheimers-disease-facts-and- figures.asp. Accessed April 8, 2013.
  • 4
    • 0030483709 scopus 로고    scopus 로고
    • Neurochemical studies of Alzheimer's disease
    • DOI 10.1006/neur.1996.0051
    • Palmer AM. Neurochemical studies of Alzheimer's disease. Neurodegeneration. 1996;5(4):381-391. (Pubitemid 27077898)
    • (1996) Neurodegeneration , vol.5 , Issue.4 , pp. 381-391
    • Palmer, A.M.1
  • 5
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus RT, Dean RL 3rd, Beer B, Lippa AS. The cholinergic hypothesis of geriatric memory dysfunction. Science. 1982;217(4558):408-414.
    • (1982) Science , vol.217 , Issue.4558 , pp. 408-414
    • Bartus, R.T.1    Dean III, R.L.2    Beer, B.3    Lippa, A.S.4
  • 6
    • 62149120882 scopus 로고    scopus 로고
    • Cell biology, regulation and inhibition of β-secretase (BACE-1)
    • Hunt CE, Turner AJ. Cell biology, regulation and inhibition of β-secretase (BACE-1). FEBS J. 2009;276(7):1845-1859.
    • (2009) FEBS J , vol.276 , Issue.7 , pp. 1845-1859
    • Hunt, C.E.1    Turner, A.J.2
  • 7
    • 78650166808 scopus 로고    scopus 로고
    • α-secretase in Alzheimer's disease: Molecular identity, regulation and therapeutic potential
    • Lichtenthaler SF. α-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potential. J Neurochem. 2011;116(1): 10-21.
    • (2011) J Neurochem , vol.116 , Issue.1 , pp. 10-21
    • Lichtenthaler, S.F.1
  • 8
    • 57649217285 scopus 로고    scopus 로고
    • The role of amyloid precursor protein processing by BACE1, the β-secretase, in Alzheimer disease pathophysiology
    • Cole SL, Vassar R. The role of amyloid precursor protein processing by BACE1, the β-secretase, in Alzheimer disease pathophysiology. J Biol Chem. 2008;283(44):29621-29625.
    • (2008) J Biol Chem , vol.283 , Issue.44 , pp. 29621-29625
    • Cole, S.L.1    Vassar, R.2
  • 10
    • 33745614108 scopus 로고    scopus 로고
    • The γ-secretase complex: Membrane-embedded proteolytic ensemble
    • DOI 10.1021/bi060799c
    • Wolfe MS. The γ-secretase complex: membrane-embedded proteolytic ensemble. Biochemistry. 2006;45(26):7931-7939. (Pubitemid 43993216)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7931-7939
    • Wolfe, M.S.1
  • 11
    • 33745853091 scopus 로고    scopus 로고
    • Presenilin-1 is an unprimed glycogen synthase kinase-3β substrate
    • DOI 10.1016/j.febslet.2006.06.035, PII S0014579306007423
    • Twomey C, McCarthy JV. Presenilin-1 is an unprimed glycogen synthase kinase-3β substrate. FEBS Lett. 2006;580(17):4015-4020. (Pubitemid 44037562)
    • (2006) FEBS Letters , vol.580 , Issue.17 , pp. 4015-4020
    • Twomey, C.1    McCarthy, J.V.2
  • 12
    • 81955167913 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase-3β mediates β-amyloid induced neuritic damage in Alzheimer's disease
    • DaRocha-Souto B, Coma M, Perez-Nievas BG, et al. Activation of glycogen synthase kinase-3β mediates β-amyloid induced neuritic damage in Alzheimer's disease. Neurobiol Dis. 2012;45(1):425-437.
    • (2012) Neurobiol Dis , vol.45 , Issue.1 , pp. 425-437
    • Darocha-Souto, B.1    Coma, M.2    Perez-Nievas, B.G.3
  • 14
    • 79952236194 scopus 로고    scopus 로고
    • Presenilin-2 mutation causes early amyloid accumulation and memory impairment in a transgenic mouse model of Alzheimer's disease
    • Toda T, Noda Y, Ito G, Maeda M, Shimizu T. Presenilin-2 mutation causes early amyloid accumulation and memory impairment in a transgenic mouse model of Alzheimer's disease. J Biomed Biotechnol. 2011;2011:617974.
    • (2011) J Biomed Biotechnol. , vol.2011 , pp. 617974
    • Toda, T.1    Noda, Y.2    Ito, G.3    Maeda, M.4    Shimizu, T.5
  • 15
    • 0034623284 scopus 로고    scopus 로고
    • Mutant presenilin 2 transgenic mice. A large increase in the levels of Aβ 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin
    • Sawamura N, Morishima-Kawashima M, Waki H, et al. Mutant presenilin 2 transgenic mice. A large increase in the levels of Aβ 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin. J Biol Chem. 2000;275(36):27901- 27908.
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 27901-27908
    • Sawamura, N.1    Morishima-Kawashima, M.2    Waki, H.3
  • 16
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • DOI 10.1126/science.274.5284.99
    • Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science. 1996;274(5284):99-102. (Pubitemid 26332733)
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 19
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 2002; 297(5580):353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 20
    • 84655162701 scopus 로고    scopus 로고
    • Twenty years of Alzheimer's disease-causing mutations
    • Goate A, Hardy J. Twenty years of Alzheimer's disease-causing mutations. J Neurochem. 2012;120(Suppl 1):3-8.
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 3-8
    • Goate, A.1    Hardy, J.2
  • 21
    • 84856541277 scopus 로고    scopus 로고
    • Rare variants in APP, PSEN1 and PSEN2 increase risk for AD in late-onset Alzheimer's disease families
    • Cruchaga C, Haller G, Chakraverty S, et al. Rare variants in APP, PSEN1 and PSEN2 increase risk for AD in late-onset Alzheimer's disease families. PloS One. 2012;7(2):e31039.
    • (2012) PloS One , vol.7 , Issue.2
    • Cruchaga, C.1    Haller, G.2    Chakraverty, S.3
  • 22
    • 0028985799 scopus 로고
    • Role of the β-amyloid protein in Alzheimer's disease
    • Sisodia SS, Price DL. Role of the β-amyloid protein in Alzheimer's disease. FASEB J. 1995;9(5):366-370.
    • (1995) FASEB J , vol.9 , Issue.5 , pp. 366-370
    • Sisodia, S.S.1    Price, D.L.2
  • 23
    • 58049155245 scopus 로고    scopus 로고
    • Amyloid β peptides in human plasma and tissues and their significance for Alzheimer's disease
    • Roher AE, Esh CL, Kokjohn TA, et al. Amyloid β peptides in human plasma and tissues and their significance for Alzheimer's disease. Alzheimers Dement. 2009;5(1):18-29.
    • (2009) Alzheimers Dement , vol.5 , Issue.1 , pp. 18-29
    • Roher, A.E.1    Esh, C.L.2    Kokjohn, T.A.3
  • 24
    • 0023737806 scopus 로고
    • A4 amyloid protein deposition and the diagnosis of Alzheimer's disease: Prevalence in aged brains determined by immunocytochemistry compared with conventional neuropathologic techniques
    • Davies L, Wolska B, Hilbich C, et al. A4 amyloid protein deposition and the diagnosis of Alzheimer's disease: prevalence in aged brains determined by immunocytochemistry compared with conventional neuropathologic techniques. Neurology. 1988;38(11):1688-1693. (Pubitemid 18265030)
    • (1988) Neurology , vol.38 , Issue.11 , pp. 1688-1693
    • Davies, L.1    Wolska, B.2    Hilbich, C.3    Multhaup, G.4    Martins, R.5    Simms, G.6    Beyreuther, K.7    Masters, C.L.8
  • 25
    • 0344441249 scopus 로고    scopus 로고
    • Amyloid β peptides and central cholinergic neurons: Functional interrelationship and relevance to Alzheimer's disease pathology
    • DOI 10.1016/S0079-6123(03)45018-8
    • Kar S, Quirion R. Amyloid β peptides and central cholinergic neurons: functional interrelationship and relevance to Alzheimer's disease pathology. Prog Brain Res. 2004;145:261-274. (Pubitemid 37442949)
    • (2004) Progress in Brain Research , vol.145 , pp. 261-274
    • Kar, S.1    Quirion, R.2
  • 26
    • 0031565991 scopus 로고    scopus 로고
    • Paired helical filament morphology varies with intracellular location in Alzheimer's disease brain
    • DOI 10.1016/S0304-3940(97)00876-8, PII S0304394097008768
    • Kurt MA, Davies DC, Kidd M. Paired helical filament morphology varies with intracellular location in Alzheimer's disease brain. Neurosci Lett. 1997;239(1):41-44. (Pubitemid 28055845)
    • (1997) Neuroscience Letters , vol.239 , Issue.1 , pp. 41-44
    • Kurt, M.A.1    Davies, D.C.2    Kidd, M.3
  • 27
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • DOI 10.1038/nrn2194, PII NRN2194
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci. 2007; 8(9):663-672. (Pubitemid 47283144)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 28
    • 84880187571 scopus 로고    scopus 로고
    • Tau protein, the paired helical filament and Alzheimer's disease
    • Goedert M, Klug A, Crowther RA. Tau protein, the paired helical filament and Alzheimer's disease. J Alzheimers Dis. 2006;9(Suppl 3): 195-207. (Pubitemid 44253313)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 195-207
    • Goedert, M.1    Klug, A.2    Crowther, R.A.3
  • 29
    • 77949267093 scopus 로고    scopus 로고
    • Amyloid β oligomers induce Ca2+ dysregulation and neuronal death through activation of ionotropic glutamate receptors
    • Alberdi E, Sanchez-Gomez MV, Cavaliere F, et al. Amyloid β oligomers induce Ca2+ dysregulation and neuronal death through activation of ionotropic glutamate receptors. Cell Calcium. 2010;47(3):264-272.
    • (2010) Cell Calcium , vol.47 , Issue.3 , pp. 264-272
    • Alberdi, E.1    Sanchez-Gomez, M.V.2    Cavaliere, F.3
  • 30
    • 0032534629 scopus 로고    scopus 로고
    • β-Amyloid binds to p75(NTR) and activates NFκB in human neuroblastoma cells
    • Kuner P, Schubenel R, Hertel C. β-amyloid binds to p57NTR and activates NFκB in human neuroblastoma cells. J Neurosci Res. 1998;54(6):798-804. (Pubitemid 28544380)
    • (1998) Journal of Neuroscience Research , vol.54 , Issue.6 , pp. 798-804
    • Kuner, P.1    Schubenel, R.2    Hertel, C.3
  • 31
    • 0032822629 scopus 로고    scopus 로고
    • Amyloid β peptide 25-35 modulates hydrolysis of phosphoinositides by membrane phospholipase(s) C of adult brain cortex
    • Strosznajder JB, Zambrzycka A, Kacprzak MD, Strosznajder RP. Amyloid β peptide 25-35 modulates hydrolysis of phosphoinositides by membrane phospholipase(s) C of adult brain cortex. J Mol Neurosci. 1999;12(2):101-109. (Pubitemid 29473323)
    • (1999) Journal of Molecular Neuroscience , vol.12 , Issue.2 , pp. 101-109
    • Strosznajder, J.B.1    Zambrzycka, A.2    Kacprzak, M.D.3    Strosznajder, R.P.4
  • 33
    • 84855866955 scopus 로고    scopus 로고
    • Oxidative stress and β-amyloid protein in Alzheimer's disease
    • Cai Z, Zhao B, Ratka A. Oxidative stress and β-amyloid protein in Alzheimer's disease. Neuromolecular Med. 2011;13(4):223-250.
    • (2011) Neuromolecular Med. , vol.13 , Issue.4 , pp. 223-250
    • Cai, Z.1    Zhao, B.2    Ratka, A.3
  • 35
    • 0032146978 scopus 로고    scopus 로고
    • The importance of inflammatory mechanisms in Alzheimer disease
    • DOI 10.1016/S0531-5565(98)00013-8, PII S0531556598000138
    • McGeer EG, McGeer PL. The importance of inflammatory mechanisms in Alzheimer disease. Exp Gerontol. 1998;33(5):371-378. (Pubitemid 28354931)
    • (1998) Experimental Gerontology , vol.33 , Issue.5 , pp. 371-378
    • McGeer, E.G.1    McGeer, P.L.2
  • 37
    • 8744276616 scopus 로고    scopus 로고
    • Amyloid β-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain
    • Butterfield DA, Boyd-Kimball D. Amyloid β-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain. Brain Pathol. 2004;14(4):426-432. (Pubitemid 39524972)
    • (2004) Brain Pathology , vol.14 , Issue.4 , pp. 426-432
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 39
    • 18044392303 scopus 로고    scopus 로고
    • Brain inflammation and oxidative stress in a transgenic mouse model of Alzheimer-like brain amyloidosis
    • Yao Y, Chinnici C, Tang H, Trojanowski JQ, Lee VM, Pratico D. Brain inflammation and oxidative stress in a transgenic mouse model of Alzheimer-like brain amyloidosis. J Neuroinflammation. 2004; 1(1):21.
    • (2004) J Neuroinflammation. , vol.1 , Issue.1 , pp. 21
    • Yao, Y.1    Chinnici, C.2    Tang, H.3    Trojanowski, J.Q.4    Lee, V.M.5    Pratico, D.6
  • 40
    • 73949134382 scopus 로고    scopus 로고
    • Population variation in oxidative stress and astrocyte DNA damage in relation to Alzheimer-type pathology in the ageing brain
    • Simpson JE, Ince PG, Haynes LJ, et al. Population variation in oxidative stress and astrocyte DNA damage in relation to Alzheimer-type pathology in the ageing brain. Neuropathol Appl Neurobiol. 2010;36(1):25-40.
    • (2010) Neuropathol Appl Neurobiol , vol.36 , Issue.1 , pp. 25-40
    • Simpson, J.E.1    Ince, P.G.2    Haynes, L.J.3
  • 41
    • 77957970155 scopus 로고    scopus 로고
    • Neuroinflammation, oxidative stress and the pathogenesis of Alzheimer's disease
    • Agostinho P, Cunha RA, Oliveira C. Neuroinflammation, oxidative stress and the pathogenesis of Alzheimer's disease. Curr Pharm Des. 2010;16(25):2766-2778.
    • (2010) Curr Pharm des , vol.16 , Issue.25 , pp. 2766-2778
    • Agostinho, P.1    Cunha, R.A.2    Oliveira, C.3
  • 42
    • 65249154212 scopus 로고    scopus 로고
    • Can treatment with nonsteroidal anti-inflammatory drugs protect from dementia?
    • Bregman N, Karni A, Korczyn AD. Can treatment with nonsteroidal anti-inflammatory drugs protect from dementia? Arch Neurol. 2009;66(4):539-540.
    • (2009) Arch Neurol , vol.66 , Issue.4 , pp. 539-540
    • Bregman, N.1    Karni, A.2    Korczyn, A.D.3
  • 43
    • 76449094399 scopus 로고    scopus 로고
    • Inflammation and anti-inflammatory strategies for Alzheimer's disease - A mini-review
    • McNaull BB, Todd S, McGuinness B, Passmore AP. Inflammation and anti-inflammatory strategies for Alzheimer's disease - a mini-review. Gerontology. 2010;56(1):3-14.
    • (2010) Gerontology , vol.56 , Issue.1 , pp. 3-14
    • McNaull, B.B.1    Todd, S.2    McGuinness, B.3    Passmore, A.P.4
  • 44
    • 67349276645 scopus 로고    scopus 로고
    • Amyloid precursor protein and α synuclein translation, implications for iron and inflammation in neurodegenerative diseases
    • Cahill CM, Lahiri DK, Huang X, Rogers JT. Amyloid precursor protein and α synuclein translation, implications for iron and inflammation in neurodegenerative diseases. Biochim Biophys Acta. 2009;1790(7): 615-628.
    • (2009) Biochim Biophys Acta. , vol.1790 , Issue.7 , pp. 615-628
    • Cahill, C.M.1    Lahiri, D.K.2    Huang, X.3    Rogers, J.T.4
  • 45
    • 77957771842 scopus 로고    scopus 로고
    • Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1
    • Cho HH, Cahill CM, Vanderburg CR, et al. Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1. J Biol Chem. 2010;285(41):31217-31232.
    • (2010) J Biol Chem , vol.285 , Issue.41 , pp. 31217-31232
    • Cho, H.H.1    Cahill, C.M.2    Vanderburg, C.R.3
  • 46
    • 46749118974 scopus 로고    scopus 로고
    • Cholinergic Treatments with Emphasis on M1 Muscarinic Agonists as Potential Disease-Modifying Agents for Alzheimer's Disease
    • DOI 10.1016/j.nurt.2008.05.002, PII S1933721308000913
    • Fisher A. Cholinergic treatments with emphasis on m1 muscarinic agonists as potential disease-modifying agents for Alzheimer's disease. Neurotherapeutics. 2008;5(3):433-442. (Pubitemid 351952486)
    • (2008) Neurotherapeutics , vol.5 , Issue.3 , pp. 433-442
    • Fisher, A.1
  • 47
    • 78651411274 scopus 로고    scopus 로고
    • Current treatments for patients with Alzheimer disease
    • Osborn GG, Saunders AV. Current treatments for patients with Alzheimer disease. J Am Osteopath Assoc. 2010;110(9 Suppl 8): S16-S26.
    • (2010) J Am Osteopath Assoc , vol.110 , Issue.9 SUPPL. 8
    • Osborn, G.G.1    Saunders, A.V.2
  • 48
  • 49
    • 42749100518 scopus 로고    scopus 로고
    • Cholinesterase inhibitors for Alzheimer's disease [review]
    • Birks J. Cholinesterase inhibitors for Alzheimer's disease [review]. Cochrane Database Syst Rev. 2006;1:CD005593.
    • (2006) Cochrane Database Syst Rev. , vol.1
    • Birks, J.1
  • 50
    • 47849119964 scopus 로고    scopus 로고
    • Efficacy and safety of donepezil, galantamine, and rivastigmine for the treatment of Alzheimer's disease: A systematic review and meta-analysis
    • Hansen RA, Gartlehner G, Webb AP, Morgan LC, Moore CG, Jonas DE. Efficacy and safety of donepezil, galantamine, and rivastigmine for the treatment of Alzheimer's disease: a systematic review and meta-analysis. Clin Interv Aging. 2008;3(2):211-225. (Pubitemid 352037861)
    • (2008) Clinical Interventions in Aging , vol.3 , Issue.2 , pp. 211-225
    • Hansen, R.A.1    Gartlehner, G.2    Webb, A.P.3    Morgan, L.C.4    Moore, C.G.5    Jonas, D.E.6
  • 51
    • 84655164275 scopus 로고    scopus 로고
    • Cholinergic modulation of amyloid precursor protein processing with emphasis on M1 muscarinic receptor: Perspectives and challenges in treatment of Alzheimer's disease
    • Fisher A. Cholinergic modulation of amyloid precursor protein processing with emphasis on M1 muscarinic receptor: perspectives and challenges in treatment of Alzheimer's disease. J Neurochem. 2012;120(Suppl 1):22-33.
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 22-33
    • Fisher, A.1
  • 52
    • 79952685399 scopus 로고    scopus 로고
    • Memantine in dementia: A review of the current evidence
    • Herrmann N, Li A, Lanctot K. Memantine in dementia: a review of the current evidence. Expert Opin Pharmacother. 2011;12(5):787-800.
    • (2011) Expert Opin Pharmacother , vol.12 , Issue.5 , pp. 787-800
    • Herrmann, N.1    Li, A.2    Lanctot, K.3
  • 55
    • 0035968057 scopus 로고    scopus 로고
    • Reduction of cerebrospinal fluid amyloid β after systemic administration of M1 muscarinic agonists
    • DOI 10.1016/S0006-8993(01)02484-2, PII S0006899301024842
    • Beach TG, Walker DG, Potter PE, Sue LI, Fisher A. Reduction of cerebrospinal fluid amyloid β after systemic administration of M1 muscarinic agonists. Brain Res. 2001;905(1-2):220-223. (Pubitemid 32553856)
    • (2001) Brain Research , vol.905 , Issue.1-2 , pp. 220-223
    • Beach, T.G.1    Walker, D.G.2    Potter, P.E.3    Sue, L.I.4    Fisher, A.5
  • 56
    • 5144234244 scopus 로고    scopus 로고
    • M1 muscarinic receptor activation protects neurons from β-amyloid toxicity. A role for Wnt signaling pathway
    • DOI 10.1016/j.nbd.2004.07.016, PII S0969996104001536
    • Farias GG, Godoy JA, Hernandez F, Avila J, Fisher A, Inestrosa NC. M1 muscarinic receptor activation protects neurons from β-amyloid toxicity. A role for Wnt signaling pathway. Neurobiol Dis. 2004;17(2):337-348. (Pubitemid 39345789)
    • (2004) Neurobiology of Disease , vol.17 , Issue.2 , pp. 337-348
    • Farias, G.G.1    Godoy, J.A.2    Hernandez, F.3    Avila, J.4    Fisher, A.5    Inestrosa, N.C.6
  • 57
    • 78649417803 scopus 로고    scopus 로고
    • Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-β production
    • Bordji K, Becerril-Ortega J, Nicole O, Buisson A. Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-β production. J Neurosci. 2010;30(47):15927-15942.
    • (2010) J Neurosci , vol.30 , Issue.47 , pp. 15927-15942
    • Bordji, K.1    Becerril-Ortega, J.2    Nicole, O.3    Buisson, A.4
  • 58
    • 80051927442 scopus 로고    scopus 로고
    • Synapses, NMDA receptor activity and neuronal Aβ production in Alzheimer's disease
    • Bordji K, Becerril-Ortega J, Buisson A. Synapses, NMDA receptor activity and neuronal Aβ production in Alzheimer's disease. Rev Neurosci. 2011;22(3):285-294.
    • (2011) Rev Neurosci , vol.22 , Issue.3 , pp. 285-294
    • Bordji, K.1    Becerril-Ortega, J.2    Buisson, A.3
  • 59
    • 33750082029 scopus 로고    scopus 로고
    • Disease modifying therapy for AD?
    • DOI 10.1111/j.1471-4159.2006.04211.x
    • Golde TE. Disease modifying therapy for AD? J Neurochem. 2006; 99(3):689-707. (Pubitemid 44583429)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.3 , pp. 689-707
    • Golde, T.E.1
  • 60
    • 55249106710 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease
    • Munoz-Torrero D. Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease. Curr Med Chem. 2008;15(24): 2433-2455.
    • (2008) Curr Med Chem , vol.15 , Issue.24 , pp. 2433-2455
    • Munoz-Torrero, D.1
  • 61
    • 10844246359 scopus 로고    scopus 로고
    • Impact of rivastigmine use on the risk of nursing home placement in a US sample
    • DOI 10.2165/00023210-200418150-00008
    • Beusterien KM, Thomas SK, Gause D, Kimel M, Arcona S, Mirski D. Impact of rivastigmine use on the risk of nursing home placement in a US sample. CNS Drugs. 2004;18(15):1143-1148. (Pubitemid 40007496)
    • (2004) CNS Drugs , vol.18 , Issue.15 , pp. 1143-1148
    • Beusterien, K.M.1    Thomas, S.K.2    Gause, D.3    Kimel, M.4    Arcona, S.5    Mirski, D.6
  • 62
  • 63
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer PL, Schulzer M, McGeer EG. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology. 1996;47(2):425-432. (Pubitemid 26324038)
    • (1996) Neurology , vol.47 , Issue.2 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 64
    • 84899501241 scopus 로고    scopus 로고
    • NSAIDs: How they work and their prospects as therapeutics in Alzheimer's disease
    • Sastre M, Gentleman SM. NSAIDs: how they work and their prospects as therapeutics in Alzheimer's disease. Front Aging Neurosci. 2010;2:20.
    • (2010) Front Aging Neurosci. , vol.2 , pp. 20
    • Sastre, M.1    Gentleman, S.M.2
  • 65
    • 70349915914 scopus 로고    scopus 로고
    • NO-flurbiprofen reduces amyloid-β, is neuroprotective in cell culture, and enhances cognition in response to cholinergic blockade
    • Abdul-Hay SO, Luo J, Ashghodom RT, Thatcher GR. NO-flurbiprofen reduces amyloid-β, is neuroprotective in cell culture, and enhances cognition in response to cholinergic blockade. J Neurochem. 2009;111(3): 766-776.
    • (2009) J Neurochem , vol.111 , Issue.3 , pp. 766-776
    • Abdul-Hay, S.O.1    Luo, J.2    Ashghodom, R.T.3    Thatcher, G.R.4
  • 66
    • 0034528414 scopus 로고    scopus 로고
    • Regulation of APP synthesis and secretion by neuroimmunophilin ligands and cyclooxygenase inhibitors
    • Lee RK, Wurtman RJ. Regulation of APP synthesis and secretion by neuroimmunophilin ligands and cyclooxygenase inhibitors. Ann N Y Acad Sci. 2000;920:261-268. (Pubitemid 32056580)
    • (2000) Annals of the New York Academy of Sciences , vol.920 , pp. 261-268
    • Lee, R.K.K.1    Wurtman, R.J.2
  • 67
    • 66349133387 scopus 로고    scopus 로고
    • Secretase inhibitors and modulators for Alzheimer's disease treatment
    • Tomita T. Secretase inhibitors and modulators for Alzheimer's disease treatment. Expert Rev Neurother. 2009;9(5):661-679.
    • (2009) Expert Rev Neurother. , vol.9 , Issue.5 , pp. 661-679
    • Tomita, T.1
  • 70
    • 47549107705 scopus 로고    scopus 로고
    • Cognitive function over time in the Alzheimer's disease anti-inflammatory prevention trial (ADAPT): Results of a randomized, controlled trial of naproxen and celecoxib
    • DOI 10.1001/archneur.2008.65.7.nct70006
    • Martin BK, Szekely C, Brandt J, et al ADAPT Research Group. Cognitive function over time in the Alzheimer's Disease Anti-inflammatory Prevention Trial (ADAPT): results of a randomized, controlled trial of naproxen and celecoxib. Arch Neurol. 2008;65(7): 896-905. (Pubitemid 352008472)
    • (2008) Archives of Neurology , vol.65 , Issue.7 , pp. 896-905
    • Martin, B.K.1    Szekely, C.2    Brandt, J.3    Piantadosi, S.4    Breitner, J.C.S.5    Craft, S.6    Evans, D.7    Green, R.8    Mullan, M.9
  • 71
    • 62849112328 scopus 로고    scopus 로고
    • Alzheimer's Disease Anti-inflammatory Prevention Trial: Design, methods, and baseline results
    • ADAPT Research Group
    • Meinert CL, McCaffrey LD, Breitner JC. ADAPT Research Group. Alzheimer's Disease Anti-inflammatory Prevention Trial: design, methods, and baseline results. Alzheimers Dement. 2009;5(2):93-104.
    • (2009) Alzheimers Dement. , vol.5 , Issue.2 , pp. 93-104
    • Meinert, C.L.1    McCaffrey, L.D.2    Breitner, J.C.3
  • 73
    • 0038375640 scopus 로고    scopus 로고
    • Effect of non-steroidal anti-inflammatory drugs on risk of Alzheimer's disease: Systematic review and meta-analysis of observational studies
    • Etminan M, Gill S, Samii A. Effect of non-steroidal anti-inflammatory drugs on risk of Alzheimer's disease: systematic review and meta-analysis of observational studies. BMJ. 2003;327(7407):128.
    • (2003) BMJ , vol.327 , Issue.7407 , pp. 128
    • Etminan, M.1    Gill, S.2    Samii, A.3
  • 75
    • 13244249900 scopus 로고    scopus 로고
    • Prevalence of dementia in an urban population in Kerala, India
    • DOI 10.1192/bjp.186.2.136
    • Shaji S, Bose S, Verghese A. Prevalence of dementia in an urban population in Kerala, India. Br J Psychiatry. 2005;186:136-140. (Pubitemid 40193783)
    • (2005) British Journal of Psychiatry , vol.186 , Issue.FEB. , pp. 136-140
    • Shaji, S.1    Bose, S.2    Verghese, A.3
  • 77
    • 83455230813 scopus 로고    scopus 로고
    • Prevalence of apolipoprotein E4 genotype and homozygotes (APOE e4/4) among patients diagnosed with Alzheimer's disease: A systematic review and meta-analysis
    • Ward A, Crean S, Mercaldi CJ, et al. Prevalence of apolipoprotein E4 genotype and homozygotes (APOE e4/4) among patients diagnosed with Alzheimer's disease: a systematic review and meta-analysis. Neuroepidemiology. 2012;38(1):1-17.
    • (2012) Neuroepidemiology , vol.38 , Issue.1 , pp. 1-17
    • Ward, A.1    Crean, S.2    Mercaldi, C.J.3
  • 81
    • 33646828805 scopus 로고    scopus 로고
    • ApoE-ε 4-dependent association of the choline acetyltransferase gene polymorphisms (2384G>A and 1882G>A) with Alzheimer's disease
    • DOI 10.1016/j.cca.2005.12.037, PII S0009898106000209
    • Ahn Jo S, Ahn K, Kim JH, et al. ApoE-ε 4-dependent association of the choline acetyltransferase gene polymorphisms (2384G. A and 1882G. A) with Alzheimer's disease. Clin Chim Acta. 2006;368(1-2): 179-182. (Pubitemid 43776017)
    • (2006) Clinica Chimica Acta , vol.368 , Issue.1-2 , pp. 179-182
    • Ahn Jo, S.1    Ahn, K.2    Kim, J.-H.3    Kang, B.-H.4    Kim, E.5    Jo, I.6    Kim, D.K.7
  • 82
    • 78650187839 scopus 로고    scopus 로고
    • Cerebrospinal fluid profile of amyloid β42 (Aβ42), hTau and ubiquitin in North Indian Alzheimer's disease patients
    • Kandimalla RJ, S P, Bk B, et al. Cerebrospinal fluid profile of amyloid β42 (Aβ42), hTau and ubiquitin in North Indian Alzheimer's disease patients. Neurosci Lett. 2011;487(2):134-138.
    • (2011) Neurosci Lett. , vol.487 , Issue.2 , pp. 134-138
    • Kandimalla, R.J.1    Bk, B.2
  • 84
    • 0029681790 scopus 로고    scopus 로고
    • Cytotoxicity and cytoprotective activities of natural compounds. The case of curcumin
    • Commandeur JN, Vermeulen NP. Cytotoxicity and cytoprotective activities of natural compounds. The case of curcumin. Xenobiotica. 1996;26(7):667-680. (Pubitemid 26233021)
    • (1996) Xenobiotica , vol.26 , Issue.7 , pp. 667-680
    • Commandeur, J.N.M.1    Vermeulen, N.P.E.2
  • 85
    • 0028134769 scopus 로고
    • Role of capsaicin, curcumin and dietary n-3 fatty acids in lowering the generation of reactive oxygen species in rat peritoneal macrophages
    • Joe B, Lokesh BR. Role of capsaicin, curcumin and dietary n-3 fatty acids in lowering the generation of reactive oxygen species in rat peritoneal macrophages. Biochim Biophys Acta. 1994;1224(2):255-263.
    • (1994) Biochim Biophys Acta , vol.1224 , Issue.2 , pp. 255-263
    • Joe, B.1    Lokesh, B.R.2
  • 86
    • 0026711273 scopus 로고
    • Studies on spice principles as antioxidants in the inhibition of lipid peroxidation of rat liver microsomes
    • Reddy AC, Lokesh BR. Studies on spice principles as antioxidants in the inhibition of lipid peroxidation of rat liver microsomes. Mol Cell Biochem. 1992;111(1-2):117-124.
    • (1992) Mol Cell Biochem , vol.111 , Issue.1-2 , pp. 117-124
    • Reddy, A.C.1    Lokesh, B.R.2
  • 87
    • 84934436057 scopus 로고    scopus 로고
    • Antioxidant and anti-inflammatory properties of curcumin
    • Menon VP, Sudheer AR. Antioxidant and anti-inflammatory properties of curcumin. Adv Exp Med Biol. 2007;595:105-125.
    • (2007) Adv Exp Med Biol. , vol.595 , pp. 105-125
    • Menon, V.P.1    Sudheer, A.R.2
  • 89
    • 59349120231 scopus 로고    scopus 로고
    • Pharmacological basis for the role of curcumin in chronic diseases: An age-old spice with modern targets
    • Aggarwal BB, Sung B. Pharmacological basis for the role of curcumin in chronic diseases: an age-old spice with modern targets. Trends Pharmacol Sci. 2009;30(2):85-94.
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.2 , pp. 85-94
    • Aggarwal, B.B.1    Sung, B.2
  • 90
    • 77955084717 scopus 로고    scopus 로고
    • Why pleiotropic interventions are needed for Alzheimer's disease
    • Frautschy SA, Cole GM. Why pleiotropic interventions are needed for Alzheimer's disease. Mol Neurobiol. 2010;41(2-3):392-409.
    • (2010) Mol Neurobiol , vol.41 , Issue.2-3 , pp. 392-409
    • Frautschy, S.A.1    Cole, G.M.2
  • 94
  • 98
    • 84863115185 scopus 로고    scopus 로고
    • Discovery of curcumin, a component of golden spice, and its miraculous biological activities
    • Gupta SC, Patchva S, Koh W, Aggarwal BB. Discovery of curcumin, a component of golden spice, and its miraculous biological activities. Clin Exp Pharm Physiol. 2012;39(3):283-299.
    • (2012) Clin Exp Pharm Physiol , vol.39 , Issue.3 , pp. 283-299
    • Gupta, S.C.1    Patchva, S.2    Koh, W.3    Aggarwal, B.B.4
  • 99
    • 0041548059 scopus 로고
    • Antibacterial action of curcumin and related compounds
    • Schraufstatter E, Bernt H. Antibacterial action of curcumin and related compounds. Nature. 1949;164(4167):456.
    • (1949) Nature , vol.164 , Issue.4167 , pp. 456
    • Schraufstatter, E.1    Bernt, H.2
  • 102
    • 78751494577 scopus 로고    scopus 로고
    • Evaluation of antiviral activities of curcumin derivatives against HSV-1 in Vero cell line
    • Zandi K, Ramedani E, Mohammadi K, et al. Evaluation of antiviral activities of curcumin derivatives against HSV-1 in Vero cell line. Nat Prod Commun. 2010;5(12):1935-1938.
    • (2010) Nat Prod Commun. , vol.5 , Issue.12 , pp. 1935-1938
    • Zandi, K.1    Ramedani, E.2    Mohammadi, K.3
  • 103
    • 79955982607 scopus 로고    scopus 로고
    • Antioxidative properties of curcumin in the protection of blood platelets against oxidative stress in vitro
    • Kolodziejczyk J, Olas B, Saluk-Juszczak J, Wachowicz B. Antioxidative properties of curcumin in the protection of blood platelets against oxidative stress in vitro. Platelets. 2011;22(4): 270-276.
    • (2011) Platelets , vol.22 , Issue.4 , pp. 270-276
    • Kolodziejczyk, J.1    Olas, B.2    Saluk-Juszczak, J.3    Wachowicz, B.4
  • 105
    • 34548058841 scopus 로고    scopus 로고
    • Curcumin, demethoxycurcumin, bisdemethoxycurcumin, tetrahydrocurcumin and turmerones differentially regulate anti-inflammatory and anti-proliferative responses through a ROS-independent mechanism
    • DOI 10.1093/carcin/bgm123
    • Sandur SK, Pandey MK, Sung B, et al. Curcumin, demethoxycurcumin, bisdemethoxycurcumin, tetrahydrocurcumin and turmerones differentially regulate anti-inflammatory and anti-proliferative responses through a ROS-independent mechanism. Carcinogenesis. 2007;28(8): 1765-1773. (Pubitemid 47289040)
    • (2007) Carcinogenesis , vol.28 , Issue.8 , pp. 1765-1773
    • Sandur, S.K.1    Pandey, M.K.2    Sung, B.3    Ahn, K.S.4    Murakami, A.5    Sethi, G.6    Limtrakul, P.7    Badmaev, V.8    Aggarwal, B.B.9
  • 106
    • 84858072552 scopus 로고    scopus 로고
    • The pharmacology of curcumin: Is it the degradation products?
    • Shen L, Ji HF. The pharmacology of curcumin: is it the degradation products? Trends Mol Med. 2012;18(3):138-144.
    • (2012) Trends Mol Med. , vol.18 , Issue.3 , pp. 138-144
    • Shen, L.1    Ji, H.F.2
  • 107
    • 0035957872 scopus 로고    scopus 로고
    • Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult
    • DOI 10.1016/S0304-3940(01)01677-9, PII S0304394001016779
    • Kim DS, Park SY, Kim JK. Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult. Neurosci Lett. 2001;303(1):57-61. (Pubitemid 32285467)
    • (2001) Neuroscience Letters , vol.303 , Issue.1 , pp. 57-61
    • Kim, D.S.1    Park, S.-Y.2    Kim, J.-Y.3
  • 108
    • 84878243573 scopus 로고    scopus 로고
    • Curcumin abates hypoxia-induced oxidative stress based-ER stress-mediated cell death in mouse hippocampal cells (HT22) by controlling Prdx6 and NF-κB regulation
    • January 30. [Epub ahead of print.]
    • Chhunchha B, Fatma N, Kubo E, Rai P, Singh SP, Singh DP. Curcumin abates hypoxia-induced oxidative stress based-ER stress-mediated cell death in mouse hippocampal cells (HT22) by controlling Prdx6 and NF-κB regulation. Am J Physiol Cell Physiol. January 30, 2013. [Epub ahead of print.]
    • (2013) Am J Physiol Cell Physiol.
    • Chhunchha, B.1    Fatma, N.2    Kubo, E.3    Rai, P.4    Singh, S.P.5    Singh, D.P.6
  • 109
    • 9744229172 scopus 로고    scopus 로고
    • Curcumin, the active constituent of turmeric, inhibits amyloid peptide-induced cytochemokine gene expression and CCR5-mediated chemotaxis of THP-1 monocytes by modulating early growth response-1 transcription factor
    • DOI 10.1111/j.1471-4159.2004.02800.x
    • Giri RK, Rajagopal V, Kalra VK. Curcumin, the active constituent of turmeric, inhibits amyloid peptide-induced cytochemokine gene expression and CCR5-mediated chemotaxis of THP-1 monocytes by modulating early growth response-1 transcription factor. J Neurochem. 2004;91(5):1199-1210. (Pubitemid 39587458)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.5 , pp. 1199-1210
    • Giri, R.K.1    Rajagopal, V.2    Kalra, V.K.3
  • 110
    • 77954383396 scopus 로고    scopus 로고
    • Potential protection of curcumin against intracellular amyloid β-induced toxicity in cultured rat prefrontal cortical neurons
    • Qin XY, Cheng Y, Yu LC. Potential protection of curcumin against intracellular amyloid β-induced toxicity in cultured rat prefrontal cortical neurons. Neurosci Lett. 2010;480(1):21-24.
    • (2010) Neurosci Lett , vol.480 , Issue.1 , pp. 21-24
    • Qin, X.Y.1    Cheng, Y.2    Yu, L.C.3
  • 111
    • 84862866441 scopus 로고    scopus 로고
    • Protective effects of curcumin on amyloid-β-induced neuronal oxidative damage
    • Huang HC, Chang P, Dai XL, Jiang ZF. Protective effects of curcumin on amyloid-β-induced neuronal oxidative damage. Neurochem Res. 2012;37(7):1584-1597.
    • (2012) Neurochem Res , vol.37 , Issue.7 , pp. 1584-1597
    • Huang, H.C.1    Chang, P.2    Dai, X.L.3    Jiang, Z.F.4
  • 112
    • 79954628955 scopus 로고    scopus 로고
    • Curcumin activates Wnt/β-catenin signaling pathway through inhibiting the activity of GSK-3β in APPswe transfected SY5Y cells
    • Zhang X, Yin WK, Shi XD, Li Y. Curcumin activates Wnt/β-catenin signaling pathway through inhibiting the activity of GSK-3β in APPswe transfected SY5Y cells. Eur J Pharm Sci. 2011;42(5):540-546.
    • (2011) Eur J Pharm Sci , vol.42 , Issue.5 , pp. 540-546
    • Zhang, X.1    Yin, W.K.2    Shi, X.D.3    Li, Y.4
  • 113
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin Has Potent Anti-Amyloidogenic Effects for Alzheimer's β-Amyloid Fibrils In Vitro
    • DOI 10.1002/jnr.20025
    • Ono K, Hasegawa K, Naiki H, Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J Neurosci Res. 2004;75(6):742-750. (Pubitemid 38296087)
    • (2004) Journal of Neuroscience Research , vol.75 , Issue.6 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 115
    • 84862498093 scopus 로고    scopus 로고
    • The effect of curcumin on the stability of Aβ dimers
    • Zhao LN, Chiu SW, Benoit J, Chew LY, Mu Y. The effect of curcumin on the stability of Aβ dimers. J Phys Chem B. 2012;116(25): 7428-7435.
    • (2012) J Phys Chem B , vol.116 , Issue.25 , pp. 7428-7435
    • Zhao, L.N.1    Chiu, S.W.2    Benoit, J.3    Chew, L.Y.4    Mu, Y.5
  • 116
    • 84858605051 scopus 로고    scopus 로고
    • A chemical analog of curcumin as an improved inhibitor of amyloid Aβ oligomerization
    • Orlando RA, Gonzales AM, Royer RE, Deck LM, Vander Jagt DL. A chemical analog of curcumin as an improved inhibitor of amyloid Aβ oligomerization. PloS One. 2012;7(3):e31869.
    • (2012) PloS One , vol.7 , Issue.3
    • Orlando, R.A.1    Gonzales, A.M.2    Royer, R.E.3    Deck, L.M.4    Vander Jagt, D.L.5
  • 117
    • 77957337974 scopus 로고    scopus 로고
    • The inhibitory effects of different curcuminoids on β-amyloid protein, β-amyloid precursor protein and β-site amyloid precursor protein cleaving enzyme 1 in swAPP HEK293 cells
    • Liu H, Li Z, Qiu D, Gu Q, Lei Q, Mao L. The inhibitory effects of different curcuminoids on β-amyloid protein, β-amyloid precursor protein and β-site amyloid precursor protein cleaving enzyme 1 in swAPP HEK293 cells. Neurosci Lett. 2010;485(2):83-88.
    • (2010) Neurosci Lett , vol.485 , Issue.2 , pp. 83-88
    • Liu, H.1    Li, Z.2    Qiu, D.3    Gu, Q.4    Lei, Q.5    Mao, L.6
  • 118
    • 77956498654 scopus 로고    scopus 로고
    • Curcumin decreases amyloid-β peptide levels by attenuating the maturation of amyloid-β precursor protein
    • Zhang C, Browne A, Child D, Tanzi RE. Curcumin decreases amyloid-β peptide levels by attenuating the maturation of amyloid-β precursor protein. J Biol Chem. 2010;285(37):28472-28480.
    • (2010) J Biol Chem , vol.285 , Issue.37 , pp. 28472-28480
    • Zhang, C.1    Browne, A.2    Child, D.3    Tanzi, R.E.4
  • 119
    • 83155181938 scopus 로고    scopus 로고
    • Curcumin mediates presenilin-1 activity to reduce β-amyloid production in a model of Alzheimer's disease
    • Zhang X, Zhang HM, Si L, Li Y. Curcumin mediates presenilin-1 activity to reduce β-amyloid production in a model of Alzheimer's disease. Pharmacol Rep. 2011;63(5):1101-1108.
    • (2011) Pharmacol Rep , vol.63 , Issue.5 , pp. 1101-1108
    • Zhang, X.1    Zhang, H.M.2    Si, L.3    Li, Y.4
  • 120
    • 58849102674 scopus 로고    scopus 로고
    • Curcumin, a cancer chemopreventive and chemotherapeutic agent, is a biologically active iron chelator
    • Jiao Y, Wilkinson J 4th, Di X, et al. Curcumin, a cancer chemopreventive and chemotherapeutic agent, is a biologically active iron chelator. Blood. 2009;113(2):462-469.
    • (2009) Blood , vol.113 , Issue.2 , pp. 462-469
    • Jiao, Y.1    Wilkinson IV, J.2    Di, X.3
  • 121
    • 84873741905 scopus 로고    scopus 로고
    • Curcumin protects against iron induced neurotoxicity in primary cortical neurons by attenuating necroptosis
    • Dai MC, Zhong ZH, Sun YH, et al. Curcumin protects against iron induced neurotoxicity in primary cortical neurons by attenuating necroptosis. Neurosci Lett. 2013;536:41-46.
    • (2013) Neurosci Lett , vol.536 , pp. 41-46
    • Dai, M.C.1    Zhong, Z.H.2    Sun, Y.H.3
  • 122
    • 4644275696 scopus 로고    scopus 로고
    • Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models
    • Baum L, Ng A. Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models. J Alzheimers Dis. 2004;6(4):367-377. (Pubitemid 39287248)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.4 , pp. 367-377
    • Baum, L.1    Ng, A.2
  • 123
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim GP, Chu T, Yang F, Beech W, Frautschy SA, Cole GM. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci. 2001;21(21): 8370-8377. (Pubitemid 33051435)
    • (2001) Journal of Neuroscience , vol.21 , Issue.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 126
    • 77955282380 scopus 로고    scopus 로고
    • Curcuminoids enhance memory in an amyloid-infused rat model of Alzheimer's disease
    • Ahmed T, Enam SA, Gilani AH. Curcuminoids enhance memory in an amyloid-infused rat model of Alzheimer's disease. Neuroscience. 2010;169(3):1296-1306.
    • (2010) Neuroscience , vol.169 , Issue.3 , pp. 1296-1306
    • Ahmed, T.1    Enam, S.A.2    Gilani, A.H.3
  • 127
    • 79959378383 scopus 로고    scopus 로고
    • A comparative study of curcuminoids to measure their effect on inflammatory and apoptotic gene expression in an Aβ plus ibotenic acid-infused rat model of Alzheimer's disease
    • Ahmed T, Gilani AH. A comparative study of curcuminoids to measure their effect on inflammatory and apoptotic gene expression in an Aβ plus ibotenic acid-infused rat model of Alzheimer's disease. Brain Res. 2011;1400:1-18.
    • (2011) Brain Res. , vol.1400 , pp. 1-18
    • Ahmed, T.1    Gilani, A.H.2
  • 128
    • 67650729973 scopus 로고    scopus 로고
    • β-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: Suppression by omega-3 fatty acids and curcumin
    • Ma QL, Yang F, Rosario ER, et al. β-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: suppression by omega-3 fatty acids and curcumin. J Neurosci. 2009;29(28):9078-9089.
    • (2009) J Neurosci , vol.29 , Issue.28 , pp. 9078-9089
    • Ma, Q.L.1    Yang, F.2    Rosario, E.R.3
  • 129
    • 38349131641 scopus 로고    scopus 로고
    • Six-month randomized, placebo-controlled, double-blind, pilot clinical trial of curcumin in patients with Alzheimer disease
    • Baum L, Lam CW, Cheung SK, et al. Six-month randomized, placebo-controlled, double-blind, pilot clinical trial of curcumin in patients with Alzheimer disease. J Clin Psychopharmacol. 2008;28(1):110-113.
    • (2008) J Clin Psychopharmacol , vol.28 , Issue.1 , pp. 110-113
    • Baum, L.1    Lam, C.W.2    Cheung, S.K.3
  • 130
    • 84867901639 scopus 로고    scopus 로고
    • Oral curcumin for Alzheimer's disease: Tolerability and efficacy in a 24-week randomized, double blind, placebo-controlled study
    • Ringman JM, Frautschy SA, Teng E, et al. Oral curcumin for Alzheimer's disease: tolerability and efficacy in a 24-week randomized, double blind, placebo-controlled study. Alzheimers Res Ther. 2012;4(5):43.
    • (2012) Alzheimers Res Ther. , vol.4 , Issue.5 , pp. 43
    • Ringman, J.M.1    Frautschy, S.A.2    Teng, E.3
  • 131
    • 77957980268 scopus 로고    scopus 로고
    • Oral curcumin for the treatment of mild-to-moderate Alzheimer's disease: Tolerability and clinical and biomarker efficacy results of a placebo-controlled 24-week study
    • Ringman JM, Cole GM, Teng E, et al. Oral curcumin for the treatment of mild-to-moderate Alzheimer's disease: tolerability and clinical and biomarker efficacy results of a placebo-controlled 24-week study. Alzheimers Dement. 2008;4(Suppl 4):T774.
    • (2008) Alzheimers Dement , vol.4 , Issue.SUPPL. 4
    • Ringman, J.M.1    Cole, G.M.2    Teng, E.3
  • 132
    • 85015469365 scopus 로고    scopus 로고
    • [homepage on the Internet]. http://www.alz.org/alzheimers-disease-facts- and-figures.asp Accessed April 8, 2013
    • www.clinicaltrials.gov [homepage on the Internet]. http://www.alz.org/ alzheimers-disease-facts-and-figures.asp Accessed April 8, 2013.
  • 133
    • 85015472271 scopus 로고    scopus 로고
    • [homepage on the Internet]. Drugs in Clinical Trials. Available from: http://www.alzforum.org/drg/drc/detail.asp?id=137. Accessed April 8, 2013
    • www.alzforum.org [homepage on the Internet]. Drugs in Clinical Trials. Available from: http://www.alzforum.org/drg/drc/detail.asp?id=137. Accessed April 8, 2013.
  • 134
    • 78751487371 scopus 로고    scopus 로고
    • Curcumin and Alzheimer disease: This marriage is not to be performed
    • Mancuso C, Siciliano R, Barone E. Curcumin and Alzheimer disease: this marriage is not to be performed. J Biol Chem. 2011; 286(3):le3.
    • (2011) J Biol Chem. , vol.286 , Issue.3
    • Mancuso, C.1    Siciliano, R.2    Barone, E.3
  • 135
    • 0035174504 scopus 로고    scopus 로고
    • Phase i clinical trial of curcumin, a chemopreventive agent, in patients with high-risk or pre-malignant lesions
    • Cheng AL, Hsu CH, Lin JK, et al. Phase I clinical trial of curcumin, a chemopreventive agent, in patients with high-risk or pre-malignant lesions. Anticancer Res. 2001;21(4B):2895-2900.
    • (2001) Anticancer Res , vol.21 , Issue.4 B , pp. 2895-2900
    • Cheng, A.L.1    Hsu, C.H.2    Lin, J.K.3
  • 136
    • 0031860081 scopus 로고    scopus 로고
    • Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers
    • DOI 10.1055/s-2006-957450
    • Shoba G, Joy D, Joseph T, Majeed M, Rajendran R, Srinivas PS. Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers. Planta Med. 1998;64(4):353-356. (Pubitemid 28234275)
    • (1998) Planta Medica , vol.64 , Issue.4 , pp. 353-356
    • Shoba, G.1    Joy, D.2    Joseph, T.3    Majeed, M.4    Rajendran, R.5    Srinivas, P.S.S.R.6
  • 138
    • 80052567229 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of curcumin analogues as multifunctional agents for the treatment of Alzheimer's disease
    • Chen SY, Chen Y, Li YP, et al. Design, synthesis, and biological evaluation of curcumin analogues as multifunctional agents for the treatment of Alzheimer's disease. Bioorg Med Chem. 2011;19(18): 5596-5604.
    • (2011) Bioorg Med Chem , vol.19 , Issue.18 , pp. 5596-5604
    • Chen, S.Y.1    Chen, Y.2    Li, Y.P.3
  • 139
    • 79955472046 scopus 로고    scopus 로고
    • Multitargeted drugs discovery: Balancing anti-amyloid and anticholinesterase capacity in a single chemical entity
    • Bolognesi ML, Bartolini M, Tarozzi A, et al. Multitargeted drugs discovery: balancing anti-amyloid and anticholinesterase capacity in a single chemical entity. Bioorg Med Chem Lett. 2011;21(9): 2655-2658.
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.9 , pp. 2655-2658
    • Bolognesi, M.L.1    Bartolini, M.2    Tarozzi, A.3
  • 140
    • 79958762040 scopus 로고    scopus 로고
    • Safety assessment of a solid lipid curcumin particle preparation: Acute and subchronic toxicity studies
    • Dadhaniya P, Patel C, Muchhara J, et al. Safety assessment of a solid lipid curcumin particle preparation: acute and subchronic toxicity studies. Food Chem Toxicol. 2011;49(8):1834-1842.
    • (2011) Food Chem Toxicol , vol.49 , Issue.8 , pp. 1834-1842
    • Dadhaniya, P.1    Patel, C.2    Muchhara, J.3
  • 141
    • 79955476046 scopus 로고    scopus 로고
    • Conjugation of curcumin onto hyaluronic acid enhances its aqueous solubility and stability
    • Manju S, Sreenivasan K. Conjugation of curcumin onto hyaluronic acid enhances its aqueous solubility and stability. J Colloid Interface Sci. 2011;359(1):318-325.
    • (2011) J Colloid Interface Sci , vol.359 , Issue.1 , pp. 318-325
    • Manju, S.1    Sreenivasan, K.2
  • 142
    • 78649442563 scopus 로고    scopus 로고
    • Hollow microcapsules built by layer by layer assembly for the encapsulation and sustained release of curcumin
    • Manju S, Sreenivasan K. Hollow microcapsules built by layer by layer assembly for the encapsulation and sustained release of curcumin. Colloids Surf B Biointerfaces. 2011;82(2):588-593.
    • (2011) Colloids Surf B Biointerfaces , vol.82 , Issue.2 , pp. 588-593
    • Manju, S.1    Sreenivasan, K.2
  • 143
    • 78650534733 scopus 로고    scopus 로고
    • Synthesis and characterization of a cytotoxic cationic polyvinylpyrrolidone-curcumin conjugate
    • Manju S, Sreenivasan K. Synthesis and characterization of a cytotoxic cationic polyvinylpyrrolidone-curcumin conjugate. J Pharm Sci. 2011;100(2):504-511.
    • (2011) J Pharm Sci. , vol.100 , Issue.2 , pp. 504-511
    • Manju, S.1    Sreenivasan, K.2
  • 144
    • 79952238275 scopus 로고    scopus 로고
    • Bioavailability enhancement of curcumin by complexation with phosphatidyl choline
    • Gupta NK, Dixit VK. Bioavailability enhancement of curcumin by complexation with phosphatidyl choline. J Pharm Sci. 2011;100(5): 1987-1995.
    • (2011) J Pharm Sci , vol.100 , Issue.5 , pp. 1987-1995
    • Gupta, N.K.1    Dixit, V.K.2
  • 145
    • 78049295075 scopus 로고    scopus 로고
    • Development and evaluation of self-microemulsifying liquid and pellet formulations of curcumin, and absorption studies in rats
    • Setthacheewakul S, Mahattanadul S, Phadoongsombut N, Pichayakorn W, Wiwattanapatapee R. Development and evaluation of self-microemulsifying liquid and pellet formulations of curcumin, and absorption studies in rats. Eur J Pharm Biopharm. 2010;76(3):475-485.
    • (2010) Eur J Pharm Biopharm. , vol.76 , Issue.3 , pp. 475-485
    • Setthacheewakul, S.1    Mahattanadul, S.2    Phadoongsombut, N.3    Pichayakorn, W.4    Wiwattanapatapee, R.5
  • 146
    • 70349902499 scopus 로고    scopus 로고
    • Evaluation of an oral carrier system in rats: Bioavailability and antioxidant properties of liposome-encapsulated curcumin
    • Takahashi M, Uechi S, Takara K, Asikin Y, Wada K. Evaluation of an oral carrier system in rats: bioavailability and antioxidant properties of liposome-encapsulated curcumin. J Agric Food Chem. 2009;57(19): 9141-9146.
    • (2009) J Agric Food Chem , vol.57 , Issue.19 , pp. 9141-9146
    • Takahashi, M.1    Uechi, S.2    Takara, K.3    Asikin, Y.4    Wada, K.5
  • 147
    • 84855856570 scopus 로고    scopus 로고
    • Gold nanoparticles generated and stabilized by water soluble curcumin-polymer conjugate: Blood compatibility evaluation and targeted drug delivery onto cancer cells
    • Manju S, Sreenivasan K. Gold nanoparticles generated and stabilized by water soluble curcumin-polymer conjugate: blood compatibility evaluation and targeted drug delivery onto cancer cells. J Colloid Interface Sci. 2012;368(1):144-151.
    • (2012) J Colloid Interface Sci. , vol.368 , Issue.1 , pp. 144-151
    • Manju, S.1    Sreenivasan, K.2
  • 148
    • 84856077097 scopus 로고    scopus 로고
    • Nanocapsulated curcumin: Oral chemopreventive formulation against diethylnitrosamine induced hepatocellular carcinoma in rat
    • Ghosh D, Choudhury ST, Ghosh S, et al. Nanocapsulated curcumin: oral chemopreventive formulation against diethylnitrosamine induced hepatocellular carcinoma in rat. Chem Biol Interact. 2012;195(3): 206-214.
    • (2012) Chem Biol Interact. , vol.195 , Issue.3 , pp. 206-214
    • Ghosh, D.1    Choudhury, S.T.2    Ghosh, S.3
  • 150
    • 67349107075 scopus 로고    scopus 로고
    • Nanoparticle encapsulation improves oral bioavailability of curcumin by at least 9-fold when compared to curcumin administered with piperine as absorption enhancer
    • Shaikh J, Ankola DD, Beniwal V, Singh D, Kumar MN. Nanoparticle encapsulation improves oral bioavailability of curcumin by at least 9-fold when compared to curcumin administered with piperine as absorption enhancer. Eur J Pharm Sci. 2009;37(3-4):223-230.
    • (2009) Eur J Pharm Sci , vol.37 , Issue.3-4 , pp. 223-230
    • Shaikh, J.1    Ankola, D.D.2    Beniwal, V.3    Singh, D.4    Kumar, M.N.5
  • 151
    • 77955873538 scopus 로고    scopus 로고
    • Fabrication of curcumin encapsulated PLGA nanoparticles for improved therapeutic effects in metastatic cancer cells
    • Yallapu MM, Gupta BK, Jaggi M, Chauhan SC. Fabrication of curcumin encapsulated PLGA nanoparticles for improved therapeutic effects in metastatic cancer cells. J Colloid Interface Sci. 2010;351(1): 19-29.
    • (2010) J Colloid Interface Sci , vol.351 , Issue.1 , pp. 19-29
    • Yallapu, M.M.1    Gupta, B.K.2    Jaggi, M.3    Chauhan, S.C.4
  • 152
    • 77953958625 scopus 로고    scopus 로고
    • The in vitro stability and in vivo pharmacokinetics of curcumin prepared as an aqueous nanoparticulate formulation
    • Mohanty C, Sahoo SK. The in vitro stability and in vivo pharmacokinetics of curcumin prepared as an aqueous nanoparticulate formulation. Biomaterials. 2010;31(25):6597-6611.
    • (2010) Biomaterials , vol.31 , Issue.25 , pp. 6597-6611
    • Mohanty, C.1    Sahoo, S.K.2
  • 153
    • 84898935659 scopus 로고    scopus 로고
    • Dendrimer-curcumin conjugate: A water soluble and effective cytotoxic agent against breast cancer cell lines
    • [Epub ahead of print.]
    • Debnath S, Saloum D, Dolai S, et al. Dendrimer-curcumin conjugate: a water soluble and effective cytotoxic agent against breast cancer cell lines. Anticancer Agents Med Chem. January 24, 2013. [Epub ahead of print.]
    • (2013) Anticancer Agents Med Chem. January , vol.24
    • Debnath, S.1    Saloum, D.2    Dolai, S.3
  • 154
    • 85015465147 scopus 로고    scopus 로고
    • Highly stabilized curcumin nanoparticles tested in an in vitro blood-brain barrier model and in Alzheimer's disease Tg2576 mice
    • [Epub ahead of print.]
    • Cheng KK, Yeung CF, Ho SW, Chow SF, Chow AH, Baum L. Highly stabilized curcumin nanoparticles tested in an in vitro blood-brain barrier model and in Alzheimer's disease Tg2576 mice. AAPS J. December 11, 2012. [Epub ahead of print.]
    • (2012) AAPS J. December , vol.11
    • Cheng, K.K.1    Yeung, C.F.2    Ho, S.W.3    Chow, S.F.4    Chow, A.H.5    Baum, L.6
  • 155
    • 77957951112 scopus 로고    scopus 로고
    • Revising the definition of Alzheimer's disease: A new lexicon
    • Dubois B, Feldman HH, Jacova C, et al. Revising the definition of Alzheimer's disease: a new lexicon. Lancet Neurol. 2010;9(11): 1118-1127.
    • (2010) Lancet Neurol , vol.9 , Issue.11 , pp. 1118-1127
    • Dubois, B.1    Feldman, H.H.2    Jacova, C.3
  • 156
    • 78751692575 scopus 로고    scopus 로고
    • Anti-Aβ therapeutics in Alzheimer's disease: The need for a paradigm shift
    • Golde TE, Schneider LS, Koo EH. Anti-Aβ therapeutics in Alzheimer's disease: the need for a paradigm shift. Neuron. 2011; 69(2):203-213.
    • (2011) Neuron , vol.69 , Issue.2 , pp. 203-213
    • Golde, T.E.1    Schneider, L.S.2    Koo, E.H.3
  • 159
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report
    • DOI 10.1038/nm840
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, Weller RO. Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report. Nat Med. 2003;9(4):448-452. (Pubitemid 36460079)
    • (2003) Nature Medicine , vol.9 , Issue.4 , pp. 448-452
    • Nicolll, J.A.R.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 160
    • 78649500577 scopus 로고    scopus 로고
    • Immunotherapy with bapineuzumab lowers CSF tau protein levels in patients with Alzheimer's disease
    • Blennow K, Zetterberg H, Wei J, Liu E, Black R, Grundman M. Immunotherapy with bapineuzumab lowers CSF tau protein levels in patients with Alzheimer's disease. Alzheimers Dement. 2010;6(Suppl 4):S134-S135.
    • (2010) Alzheimers Dement , vol.6 , Issue.SUPPL. 4
    • Blennow, K.1    Zetterberg, H.2    Wei, J.3    Liu, E.4    Black, R.5    Grundman, M.6
  • 161
    • 77953742092 scopus 로고    scopus 로고
    • A phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease
    • Laskowitz DT, Kolls BJ. A phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease. Neurology. 2010;74(24):2026.
    • (2010) Neurology , vol.74 , Issue.24 , pp. 2026
    • Laskowitz, D.T.1    Kolls, B.J.2
  • 162
    • 76849103927 scopus 로고    scopus 로고
    • Identification, characterization, and comparison of amino-terminally truncated Aβ42 peptides in Alzheimer's disease brain tissue and in plasma from Alzheimer's patients receiving solanezumab immunotherapy treatment
    • DeMattos RB, Racke MM, Gelfanova V, et al. Identification, characterization, and comparison of amino-terminally truncated Aβ42 peptides in Alzheimer's disease brain tissue and in plasma from Alzheimer's patients receiving solanezumab immunotherapy treatment. Alzheimers Dement. 2009;5(Suppl 4):P156-P157.
    • (2009) Alzheimers Dement. , vol.5 , Issue.SUPPL. 4
    • Demattos, R.B.1    Racke, M.M.2    Gelfanova, V.3
  • 163
    • 66749084437 scopus 로고    scopus 로고
    • A γ-secretase inhibitor decreases amyloid-β production in the central nervous system
    • Bateman RJ, Siemers ER, Mawuenyega KG, et al. A γ-secretase inhibitor decreases amyloid-β production in the central nervous system. Ann Neurol. 2009;66(1):48-54.
    • (2009) Ann Neurol. , vol.66 , Issue.1 , pp. 48-54
    • Bateman, R.J.1    Siemers, E.R.2    Mawuenyega, K.G.3
  • 165
    • 78649504377 scopus 로고    scopus 로고
    • Formulation of a medical food cocktail for Alzheimer's disease: Beneficial effects on cognition and neuropathology in a mouse model of the disease
    • Parachikova A, Green KN, Hendrix C, LaFerla FM. Formulation of a medical food cocktail for Alzheimer's disease: beneficial effects on cognition and neuropathology in a mouse model of the disease. PloS One. 2010;5(11):e14015.
    • (2010) PloS One , vol.5 , Issue.11
    • Parachikova, A.1    Green, K.N.2    Hendrix, C.3    Laferla, F.M.4


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