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Volumn 12, Issue 2, 2012, Pages 180-188

Vitamin A and Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid protein; Oligomer; VitaminA

Indexed keywords

AMYLOID BETA PROTEIN; BETA CAROTENE; RETINAL; RETINOIC ACID; RETINOL;

EID: 84859004158     PISSN: 14441586     EISSN: 14470594     Source Type: Journal    
DOI: 10.1111/j.1447-0594.2011.00786.x     Document Type: Review
Times cited : (111)

References (91)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001; 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 0033850870 scopus 로고    scopus 로고
    • Pharmacological treatment of Alzheimer disease: from psychotropic drugs and cholinesterase inhibitors to pharmacogenomics
    • Cacabelos R, Alvarez A, Lombardi A etal. Pharmacological treatment of Alzheimer disease: from psychotropic drugs and cholinesterase inhibitors to pharmacogenomics. Drugs Today 2000; 36: 415-499.
    • (2000) Drugs Today , vol.36 , pp. 415-499
    • Cacabelos, R.1    Alvarez, A.2    Lombardi, A.3
  • 3
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimer's disease
    • Melnikova I. Therapies for Alzheimer's disease. Nat Rev Drug Discov 2007; 6: 341-342.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 341-342
    • Melnikova, I.1
  • 4
    • 77957017871 scopus 로고    scopus 로고
    • The development of new therapeutics for Alzheimer's disease
    • Carter MD, Simms GA, Weaver DF. The development of new therapeutics for Alzheimer's disease. Clin Pharmacol Ther 2010; 88: 475-486.
    • (2010) Clin Pharmacol Ther , vol.88 , pp. 475-486
    • Carter, M.D.1    Simms, G.A.2    Weaver, D.F.3
  • 5
    • 11444267243 scopus 로고    scopus 로고
    • Evaluation of the safety and immunogenicity of synthetic Aβ42 (AN1792) in patients with AD
    • Bayer AJ, Bullock R, Jones RW etal. Evaluation of the safety and immunogenicity of synthetic Aβ42 (AN1792) in patients with AD. Neurology 2005; 64: 94-101.
    • (2005) Neurology , vol.64 , pp. 94-101
    • Bayer, A.J.1    Bullock, R.2    Jones, R.W.3
  • 6
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
    • Gilman S, Koller M, Black RS etal. Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial. Neurology 2005; 64: 1553-1562.
    • (2005) Neurology , vol.64 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.S.3
  • 7
    • 0034700471 scopus 로고    scopus 로고
    • Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J etal. Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 2000; 408: 979-982.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3
  • 8
    • 84984755327 scopus 로고    scopus 로고
    • Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan D, Diamond DM, Gottschall PE etal. Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 2000; 408: 982-985.
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3
  • 9
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Aβ42 immunization
    • Orgogozo JM, Gilman S, Dartigues JF etal. Subacute meningoencephalitis in a subset of patients with AD after Aβ42 immunization. Neurology 2003; 61: 46-54.
    • (2003) Neurology , vol.61 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3
  • 10
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W etal. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999; 400: 173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 11
    • 79551633353 scopus 로고    scopus 로고
    • β-secretase inhibitor GRL-8234 rescues age-related cognitive decline in APP transgenic mice
    • Chang WP, Huang X, Downs D etal. β-secretase inhibitor GRL-8234 rescues age-related cognitive decline in APP transgenic mice. FASEB J 2011; 25: 775-784.
    • (2011) FASEB J , vol.25 , pp. 775-784
    • Chang, W.P.1    Huang, X.2    Downs, D.3
  • 12
    • 79952529991 scopus 로고    scopus 로고
    • What the halted phase III gamma-secretase inhibitor trial may (or may not) be telling us
    • Schor NF. What the halted phase III gamma-secretase inhibitor trial may (or may not) be telling us. Ann Neurol 2011; 69: 237-239.
    • (2011) Ann Neurol , vol.69 , pp. 237-239
    • Schor, N.F.1
  • 13
    • 0034192158 scopus 로고    scopus 로고
    • B-secretase revealed: starting gate for race to novel therapies for Alzheimer's disease
    • Skovronsky DM, Lee VM. B-secretase revealed: starting gate for race to novel therapies for Alzheimer's disease. Trends Pharmacol Sci 2000; 21: 161-163.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 161-163
    • Skovronsky, D.M.1    Lee, V.M.2
  • 14
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S etal. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999; 286: 735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 15
    • 0030000385 scopus 로고    scopus 로고
    • The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease
    • Breitner JC. The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease. Annu Rev Med 1996; 47: 401-411.
    • (1996) Annu Rev Med , vol.47 , pp. 401-411
    • Breitner, J.C.1
  • 16
    • 33750198829 scopus 로고    scopus 로고
    • Gamma-secretase modulation with Aβ42-lowering nonsteroidal anti-inflammatory drugs and derived compounds
    • Czirr E, Weggen S. Gamma-secretase modulation with Aβ42-lowering nonsteroidal anti-inflammatory drugs and derived compounds. Neurodegener Dis 2006; 3: 298-304.
    • (2006) Neurodegener Dis , vol.3 , pp. 298-304
    • Czirr, E.1    Weggen, S.2
  • 17
    • 45149105232 scopus 로고    scopus 로고
    • Substrate-targeting gamma-secretase modulators
    • Kukar TL, Ladd TB, Bann MA etal. Substrate-targeting gamma-secretase modulators. Nature 2008; 453: 925-929.
    • (2008) Nature , vol.453 , pp. 925-929
    • Kukar, T.L.1    Ladd, T.B.2    Bann, M.A.3
  • 18
    • 0345830739 scopus 로고    scopus 로고
    • Rofecoxib: no effect on Alzheimer's disease in a 1-year, randomized, blinded, controlled study
    • Reines SA, Block GA, Morris JC etal. Rofecoxib: no effect on Alzheimer's disease in a 1-year, randomized, blinded, controlled study. Neurology 2004; 62: 66-71.
    • (2004) Neurology , vol.62 , pp. 66-71
    • Reines, S.A.1    Block, G.A.2    Morris, J.C.3
  • 19
    • 0037167542 scopus 로고    scopus 로고
    • Reduced incidence of AD with NSAID but not H2 receptor antagonists: the Cache County Study
    • Zandi PP, Anthony JC, Hayden KM, Mehta K, Mayer L, Breitner JC. Reduced incidence of AD with NSAID but not H2 receptor antagonists: the Cache County Study. Neurology 2002; 59: 880-886.
    • (2002) Neurology , vol.59 , pp. 880-886
    • Zandi, P.P.1    Anthony, J.C.2    Hayden, K.M.3    Mehta, K.4    Mayer, L.5    Breitner, J.C.6
  • 20
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies
    • Kirkitadze MD, Bitan G, Teplow DB. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J Neurosci Res 2002; 69: 567-577.
    • (2002) J Neurosci Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 21
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - a decade of discovery
    • Walsh DM, Selkoe DJ. Aβ oligomers - a decade of discovery. J Neurochem 2007; 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 22
    • 0027730459 scopus 로고
    • Adult rabbit brain synthesizes retinoic acid
    • Dev S, Adler AJ, Edwards RB. Adult rabbit brain synthesizes retinoic acid. Brain Res 1993; 632: 325-328.
    • (1993) Brain Res , vol.632 , pp. 325-328
    • Dev, S.1    Adler, A.J.2    Edwards, R.B.3
  • 23
    • 0028341128 scopus 로고
    • Hot spots of retinoic acid synthesis in the developing spinal cord
    • McCaffery P, Drager UC. Hot spots of retinoic acid synthesis in the developing spinal cord. Proc Natl Acad Sci U S A 1994; 91: 7194-7197.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7194-7197
    • McCaffery, P.1    Drager, U.C.2
  • 24
    • 0025964109 scopus 로고
    • Differentially expressed isoforms of the mouse retinoic acid receptor β generated by usage of two promoters and alternative splicing
    • Zelent A, Mendelsohn C, Kastner P etal. Differentially expressed isoforms of the mouse retinoic acid receptor β generated by usage of two promoters and alternative splicing. EMBO J 1991; 10: 71-81.
    • (1991) EMBO J , vol.10 , pp. 71-81
    • Zelent, A.1    Mendelsohn, C.2    Kastner, P.3
  • 25
    • 70849097441 scopus 로고    scopus 로고
    • All-trans retinoic acid as a novel therapeutic strategy for Alzheimer's disease
    • Lee HP, Casadesus G, Zhu X etal. All-trans retinoic acid as a novel therapeutic strategy for Alzheimer's disease. Expert Rev Neurother 2009; 9: 1615-1621.
    • (2009) Expert Rev Neurother , vol.9 , pp. 1615-1621
    • Lee, H.P.1    Casadesus, G.2    Zhu, X.3
  • 26
    • 0034914927 scopus 로고    scopus 로고
    • Antioxidant defences and oxidative stress markers in erythrocytes and plasma from normally nourished elderly Alzheimer patients
    • Bourdel-Marchasson I, Delmas-Beauvieux MC, Peuchant E etal. Antioxidant defences and oxidative stress markers in erythrocytes and plasma from normally nourished elderly Alzheimer patients. Age Ageing 2001; 30: 235-241.
    • (2001) Age Ageing , vol.30 , pp. 235-241
    • Bourdel-Marchasson, I.1    Delmas-Beauvieux, M.C.2    Peuchant, E.3
  • 27
    • 0032921546 scopus 로고    scopus 로고
    • Plasma chain-breaking antioxidants in Alzheimer's disease, vascular dementia and Parkinson's disease
    • Foy CJ, Passmore AP, Vahidassr MD, Young IS, Lawson JT. Plasma chain-breaking antioxidants in Alzheimer's disease, vascular dementia and Parkinson's disease. QJM 1999; 92: 39-45.
    • (1999) QJM , vol.92 , pp. 39-45
    • Foy, C.J.1    Passmore, A.P.2    Vahidassr, M.D.3    Young, I.S.4    Lawson, J.T.5
  • 29
    • 0032799243 scopus 로고    scopus 로고
    • Serum levels of β-carotene, α-carotene and vitamin A in patients with Alzheimer's disease
    • Jimenez-Jimenez FJ, Molina JA, de Bustos F etal. Serum levels of β-carotene, α-carotene and vitamin A in patients with Alzheimer's disease. Eur J Neurol 1999; 6: 495-497.
    • (1999) Eur J Neurol , vol.6 , pp. 495-497
    • Jimenez-Jimenez, F.J.1    Molina, J.A.2    de Bustos, F.3
  • 31
    • 0030949126 scopus 로고    scopus 로고
    • The relation between antioxidants and memory performance in the old and very old
    • Perrig WJ, Perrig P, Stahelin HB. The relation between antioxidants and memory performance in the old and very old. J Am Geriatr Soc 1997; 45: 718-724.
    • (1997) J Am Geriatr Soc , vol.45 , pp. 718-724
    • Perrig, W.J.1    Perrig, P.2    Stahelin, H.B.3
  • 32
    • 9544248763 scopus 로고    scopus 로고
    • Dietary antioxidants and cognitive function in a population-based sample of older persons. The Rotterdam Study
    • Jama JW, Launer LJ, Witteman JC etal. Dietary antioxidants and cognitive function in a population-based sample of older persons. The Rotterdam Study. Am J Epidemiol 1996; 144: 275-280.
    • (1996) Am J Epidemiol , vol.144 , pp. 275-280
    • Jama, J.W.1    Launer, L.J.2    Witteman, J.C.3
  • 33
    • 4544227975 scopus 로고    scopus 로고
    • Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M. Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro. Exp Neurol 2004; 189: 380-392.
    • (2004) Exp Neurol , vol.189 , pp. 380-392
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 34
    • 81855199775 scopus 로고    scopus 로고
    • Vitamin A has Anti-Oligomerization effects on Amyloid-β in vitro
    • Takasaki J, Ono K, Yoshiike Y etal. Vitamin A has Anti-Oligomerization effects on Amyloid-β in vitro. J Alzheimers Dis 2011; 27: 271-280.
    • (2011) J Alzheimers Dis , vol.27 , pp. 271-280
    • Takasaki, J.1    Ono, K.2    Yoshiike, Y.3
  • 35
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984; 122: 1131-1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 36
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120: 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 37
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D, Lerman MI, McBride OW, Saffiotti U, Gajdusek DC. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 1987; 235: 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 38
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A etal. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325: 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 39
    • 0023109592 scopus 로고
    • Amyloid β protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus
    • Tanzi RE, Gusella JF, Watkins PC etal. Amyloid β protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Science 1987; 235: 880-884.
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3
  • 40
    • 0014481635 scopus 로고
    • Presenile dementia and Alzheimer's disease in mongolism
    • Olson MI, Shaw CM. Presenile dementia and Alzheimer's disease in mongolism. Brain 1969; 92: 147-156.
    • (1969) Brain , vol.92 , pp. 147-156
    • Olson, M.I.1    Shaw, C.M.2
  • 41
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E, Wasco W, Poorkaj P etal. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 1995; 269: 973-977.
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 42
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev EI, Sherrington R, Rogaeva EA etal. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 1995; 376: 775-778.
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 43
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R, Rogaev EI, Liang Y etal. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 1995; 375: 754-760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 44
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper B, Saftig P, Craessaerts K etal. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 1998; 391: 387-390.
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 45
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999; 398: 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 46
    • 0028169925 scopus 로고
    • Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43). Neuron 1994; 13: 45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 47
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • Miller DL, Papayannopoulos IA, Styles J etal. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 1993; 301: 41-52.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3
  • 48
    • 0027332081 scopus 로고
    • β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease
    • Roher AE, Lowenson JD, Clarke S etal. β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc Natl Acad Sci U S A 1993; 90: 10836-10840.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 49
    • 0034718027 scopus 로고    scopus 로고
    • Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease
    • Golde TE, Eckman CB, Younkin SG. Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease. Biochim Biophys Acta 2000; 1502: 172-187.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 172-187
    • Golde, T.E.1    Eckman, C.B.2    Younkin, S.G.3
  • 50
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT Jr. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993; 32: 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr, P.T.3
  • 51
    • 22544482926 scopus 로고    scopus 로고
    • Aβ42 is essential for parenchymal and vascular amyloid deposition in mice
    • McGowan E, Pickford F, Kim J etal. Aβ42 is essential for parenchymal and vascular amyloid deposition in mice. Neuron 2005; 47: 191-199.
    • (2005) Neuron , vol.47 , pp. 191-199
    • McGowan, E.1    Pickford, F.2    Kim, J.3
  • 52
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 2007; 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 53
    • 79952563494 scopus 로고    scopus 로고
    • Low-n oligomers as therapeutic targets of Alzheimer's disease
    • Ono K, Yamada M. Low-n oligomers as therapeutic targets of Alzheimer's disease. J Neurochem 2011; 117: 19-28.
    • (2011) J Neurochem , vol.117 , pp. 19-28
    • Ono, K.1    Yamada, M.2
  • 54
    • 0037098866 scopus 로고    scopus 로고
    • Antioxidant neuroprotection in Alzheimer's disease as preventive and therapeutic approach
    • Behl C, Moosmann B. Antioxidant neuroprotection in Alzheimer's disease as preventive and therapeutic approach. Free Radic Biol Med 2002; 33: 182-191.
    • (2002) Free Radic Biol Med , vol.33 , pp. 182-191
    • Behl, C.1    Moosmann, B.2
  • 55
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature 2000; 408: 239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 56
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson MP. Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 1997; 77: 1081-1132.
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 57
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr, P.T.2
  • 59
    • 0030977663 scopus 로고    scopus 로고
    • Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's β-amyloid fibril formation in vitro
    • Naiki H, Gejyo F, Nakakuki K. Concentration-dependent inhibitory effects of apolipoprotein E on Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 1997; 36: 6243-6250.
    • (1997) Biochemistry , vol.36 , pp. 6243-6250
    • Naiki, H.1    Gejyo, F.2    Nakakuki, K.3
  • 60
    • 33745173188 scopus 로고    scopus 로고
    • Anti-amyloidogenic effects of antioxidants: implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K, Hamaguchi T, Naiki H, Yamada M. Anti-amyloidogenic effects of antioxidants: implications for the prevention and therapeutics of Alzheimer's disease. Biochim Biophys Acta 2006; 1762: 575-586.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 575-586
    • Ono, K.1    Hamaguchi, T.2    Naiki, H.3    Yamada, M.4
  • 61
    • 0030024717 scopus 로고    scopus 로고
    • In vitro growth of Alzheimer's disease β-amyloid plaques displays first-order kinetics
    • Esler WP, Stimson ER, Ghilardi JR etal. In vitro growth of Alzheimer's disease β-amyloid plaques displays first-order kinetics. Biochemistry 1996; 35: 749-757.
    • (1996) Biochemistry , vol.35 , pp. 749-757
    • Esler, W.P.1    Stimson, E.R.2    Ghilardi, J.R.3
  • 62
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H, Nakakuki K. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab Invest 1996; 74: 374-383.
    • (1996) Lab Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 63
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 1997; 272: 22364-22372.
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 64
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh DM, Hartley DM, Kusumoto Y etal. Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999; 274: 25945-25952.
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3
  • 65
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP etal. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 1999; 19: 8876-8884.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3
  • 66
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid β-protein into sodium dodecyl sulfate-stable oligomers in cell culture
    • Podlisny MB, Ostaszewski BL, Squazzo SL etal. Aggregation of secreted amyloid β-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J Biol Chem 1995; 270: 9564-9570.
    • (1995) J Biol Chem , vol.270 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3
  • 67
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV etal. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 68
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
    • Cleary JP, Walsh DM, Hofmeister JJ etal. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat Neurosci 2005; 8: 79-84.
    • (2005) Nat Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 69
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ. Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers. J Physiol 2006; 572: 477-492.
    • (2006) J Physiol , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 70
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH etal. Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 2008; 14: 837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3
  • 71
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li S, Hong S, Shepardson NE, Walsh DM, Shankar GM, Selkoe D. Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 2009; 62: 788-801.
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 72
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid β-protein oligomers
    • Ono K, Condron MM, Teplow DB. Structure-neurotoxicity relationships of amyloid β-protein oligomers. Proc Natl Acad Sci U S A 2009; 106: 14745-14750.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 73
    • 33144487701 scopus 로고    scopus 로고
    • Temporal profile of amyloid-β (Aβ) oligomerization in an in vivo model of Alzheimer disease. A link between Aβ and tau pathology
    • Oddo S, Caccamo A, Tran L etal. Temporal profile of amyloid-β (Aβ) oligomerization in an in vivo model of Alzheimer disease. A link between Aβ and tau pathology. J Biol Chem 2006; 281: 1599-1604.
    • (2006) J Biol Chem , vol.281 , pp. 1599-1604
    • Oddo, S.1    Caccamo, A.2    Tran, L.3
  • 74
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 2009; 457: 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 75
    • 76649093635 scopus 로고    scopus 로고
    • Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
    • Balducci C, Beeg M, Stravalaci M etal. Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein. Proc Natl Acad Sci U S A 2010; 107: 2295-2300.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2295-2300
    • Balducci, C.1    Beeg, M.2    Stravalaci, M.3
  • 76
    • 77956165325 scopus 로고    scopus 로고
    • Prion protein and Aβ-related synaptic toxicity impairment
    • Calella AM, Farinelli M, Nuvolone M etal. Prion protein and Aβ-related synaptic toxicity impairment. EMBO Mol Med 2010; 2: 306-314.
    • (2010) EMBO Mol Med , vol.2 , pp. 306-314
    • Calella, A.M.1    Farinelli, M.2    Nuvolone, M.3
  • 77
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-β (Aβ) oligomers: role OF N-terminal residues
    • Chen S, Yadav SP, Surewicz WK. Interaction between human prion protein and amyloid-β (Aβ) oligomers: role OF N-terminal residues. J Biol Chem 2010; 285: 26377-26383.
    • (2010) J Biol Chem , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 78
    • 79958249995 scopus 로고    scopus 로고
    • Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites
    • Freir DB, Nicoll AJ, Klyubin I etal. Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites. Nat Commun 2011; 2: 336.
    • (2011) Nat Commun , vol.2 , pp. 336
    • Freir, D.B.1    Nicoll, A.J.2    Klyubin, I.3
  • 80
    • 0033605523 scopus 로고    scopus 로고
    • Vitamin E and β-carotene protect against ethanol combined with ischemia in an embryonic rat hippocampal culture model of fetal alcohol syndrome
    • Mitchell JJ, Paiva M, Heaton MB. Vitamin E and β-carotene protect against ethanol combined with ischemia in an embryonic rat hippocampal culture model of fetal alcohol syndrome. Neurosci Lett 1999; 263: 189-192.
    • (1999) Neurosci Lett , vol.263 , pp. 189-192
    • Mitchell, J.J.1    Paiva, M.2    Heaton, M.B.3
  • 81
    • 0033048731 scopus 로고    scopus 로고
    • The antioxidants vitamin E and β-carotene protect against ethanol-induced neurotoxicity in embryonic rat hippocampal cultures
    • Mitchell JJ, Paiva M, Heaton MB. The antioxidants vitamin E and β-carotene protect against ethanol-induced neurotoxicity in embryonic rat hippocampal cultures. Alcohol 1999; 17: 163-168.
    • (1999) Alcohol , vol.17 , pp. 163-168
    • Mitchell, J.J.1    Paiva, M.2    Heaton, M.B.3
  • 82
    • 0033992544 scopus 로고    scopus 로고
    • Inhibition of glutathione depletion by retinoic acid and tocopherol protects cultured neurons from staurosporine-induced oxidative stress and apoptosis
    • Ahlemeyer B, Krieglstein J. Inhibition of glutathione depletion by retinoic acid and tocopherol protects cultured neurons from staurosporine-induced oxidative stress and apoptosis. Neurochem Int 2000; 36: 1-5.
    • (2000) Neurochem Int , vol.36 , pp. 1-5
    • Ahlemeyer, B.1    Krieglstein, J.2
  • 83
    • 21744440266 scopus 로고    scopus 로고
    • Retinoic acid isomers protect hippocampal neurons from amyloid-β induced neurodegeneration
    • Sahin M, Karauzum SB, Perry G, Smith MA, Aliciguzel Y. Retinoic acid isomers protect hippocampal neurons from amyloid-β induced neurodegeneration. Neurotox Res 2005; 7: 243-250.
    • (2005) Neurotox Res , vol.7 , pp. 243-250
    • Sahin, M.1    Karauzum, S.B.2    Perry, G.3    Smith, M.A.4    Aliciguzel, Y.5
  • 84
    • 0035949512 scopus 로고    scopus 로고
    • Vitamin A deprivation results in reversible loss of hippocampal long-term synaptic plasticity
    • Misner DL, Jacobs S, Shimizu Y etal. Vitamin A deprivation results in reversible loss of hippocampal long-term synaptic plasticity. Proc Natl Acad Sci U S A 2001; 98: 11714-11719.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11714-11719
    • Misner, D.L.1    Jacobs, S.2    Shimizu, Y.3
  • 85
    • 0037146706 scopus 로고    scopus 로고
    • Vitamin A deficiency produces spatial learning and memory impairment in rats
    • Cocco S, Diaz G, Stancampiano R etal. Vitamin A deficiency produces spatial learning and memory impairment in rats. Neuroscience 2002; 115: 475-482.
    • (2002) Neuroscience , vol.115 , pp. 475-482
    • Cocco, S.1    Diaz, G.2    Stancampiano, R.3
  • 86
    • 0141645549 scopus 로고    scopus 로고
    • Vitamin A deficiency and relational memory deficit in adult mice: relationships with changes in brain retinoid signalling
    • Etchamendy N, Enderlin V, Marighetto A, Pallet V, Higueret P, Jaffard R. Vitamin A deficiency and relational memory deficit in adult mice: relationships with changes in brain retinoid signalling. Behav Brain Res 2003; 145: 37-49.
    • (2003) Behav Brain Res , vol.145 , pp. 37-49
    • Etchamendy, N.1    Enderlin, V.2    Marighetto, A.3    Pallet, V.4    Higueret, P.5    Jaffard, R.6
  • 87
    • 4344628460 scopus 로고    scopus 로고
    • Disruption of the retinoid signalling pathway causes a deposition of amyloid β in the adult rat brain
    • Corcoran JP, So PL, Maden M. Disruption of the retinoid signalling pathway causes a deposition of amyloid β in the adult rat brain. Eur J Neurosci 2004; 20: 896-902.
    • (2004) Eur J Neurosci , vol.20 , pp. 896-902
    • Corcoran, J.P.1    So, P.L.2    Maden, M.3
  • 88
    • 58149268892 scopus 로고    scopus 로고
    • Retinoic acid attenuates β-amyloid deposition and rescues memory deficits in an Alzheimer's disease transgenic mouse model
    • Ding Y, Qiao A, Wang Z etal. Retinoic acid attenuates β-amyloid deposition and rescues memory deficits in an Alzheimer's disease transgenic mouse model. J Neurosci 2008; 28: 11622-11634.
    • (2008) J Neurosci , vol.28 , pp. 11622-11634
    • Ding, Y.1    Qiao, A.2    Wang, Z.3
  • 89
    • 0037418321 scopus 로고    scopus 로고
    • Evidence for defective retinoid transport and function in late onsheimer's disease
    • Goodman AB, Pardee AB. Evidence for defective retinoid transport and function in late onset Alzheimer's disease. Proc Natl Acad Sci U S A 2003; 100: 2901-2905.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2901-2905
    • Goodman, A.B.1    Pardee, A.B.2
  • 90
    • 0021923812 scopus 로고
    • Restricted transport of vitamin D and A derivatives through the rat blood-brain barrier
    • Pardridge WM, Sakiyama R, Coty WA. Restricted transport of vitamin D and A derivatives through the rat blood-brain barrier. J Neurochem 1985; 44: 1138-1141.
    • (1985) J Neurochem , vol.44 , pp. 1138-1141
    • Pardridge, W.M.1    Sakiyama, R.2    Coty, W.A.3
  • 91
    • 0036087066 scopus 로고    scopus 로고
    • Retinoic acid is detected at relatively high levels in the CNS of adult rats
    • Werner EA, Deluca HF. Retinoic acid is detected at relatively high levels in the CNS of adult rats. Am J Physiol Endocrinol Metab 2002; 282: E672-E678.
    • (2002) Am J Physiol Endocrinol Metab , vol.282
    • Werner, E.A.1    Deluca, H.F.2


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