메뉴 건너뛰기




Volumn 123, Issue 12, 2013, Pages 823-831

Establishment of experimental models for Alzheimer's disease research

Author keywords

AD pathology; Alzheimer's disease (AD); Experimental model

Indexed keywords

ALUMINUM CHLORIDE; AMYLOID; APOMORPHINE; BETA SECRETASE 1; CHOLESTEROL; COPPER; DANTROLENE; DIMEBON; GALACTOSE; GAMMA SECRETASE; GREEN FLUORESCENT PROTEIN; MAGNESIUM; TAU PROTEIN;

EID: 84887927271     PISSN: 00207454     EISSN: 15635279     Source Type: Journal    
DOI: 10.3109/00207454.2013.804821     Document Type: Article
Times cited : (7)

References (100)
  • 1
    • 33846179357 scopus 로고    scopus 로고
    • Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline
    • Waldemar G, Dubois B, Emre M, et al. Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline. Eur J Neurol 2007;14:e1-26.
    • (2007) Eur J Neurol , vol.14
    • Waldemar, G.1    Dubois, B.2    Emre, M.3
  • 4
    • 80053912909 scopus 로고    scopus 로고
    • Alzheimer's disease: Beta-amyloid plaque formation in human brain
    • Seeman P, Seeman N. Alzheimer's disease: beta-amyloid plaque formation in human brain. Synapse 2011;65:1289-97.
    • (2011) Synapse , vol.65 , pp. 1289-1297
    • Seeman, P.1    Seeman, N.2
  • 5
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992;256:184-5.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 6
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 2007;8:663-72.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 7
    • 1642270170 scopus 로고    scopus 로고
    • Meat-adaptive genes and the evolution of slower aging in humans
    • Finch CE, Stanford CB. Meat-adaptive genes and the evolution of slower aging in humans. Q Rev Biol 2004;79:3- 50.
    • (2004) Q Rev Biol , vol.79 , pp. 3-50
    • Finch, C.E.1    Stanford, C.B.2
  • 8
    • 47049120305 scopus 로고    scopus 로고
    • Tauopathy with paired helical filaments in an aged chimpanzee
    • Rosen RF, Farberg AS, Gearing M, et al. Tauopathy with paired helical filaments in an aged chimpanzee. J CompNeurol 2008;509:259-70.
    • (2008) J CompNeurol , vol.509 , pp. 259-270
    • Rosen, R.F.1    Farberg, A.S.2    Gearing, M.3
  • 9
    • 0035984815 scopus 로고    scopus 로고
    • Brain clearance of Alzheimer's amyloid-beta40 in the squirrel monkey: A SPECT study in a primate model of cerebral amyloid angiopathy
    • Bading JR, Yamada S, Mackic JB, et al. Brain clearance of Alzheimer's amyloid-beta40 in the squirrel monkey: a SPECT study in a primate model of cerebral amyloid angiopathy. J Drug Target 2002;10:359-68.
    • (2002) J Drug Target , vol.10 , pp. 359-368
    • Bading, J.R.1    Yamada, S.2    Mackic, J.B.3
  • 10
    • 64549150594 scopus 로고    scopus 로고
    • Natural non-transgenic animal models for research in Alzheimer's disease
    • Sarasa M, Pesini P. Natural non-transgenic animal models for research in Alzheimer's disease. Curr Alzheimer Res 2009;6:171-8.
    • (2009) Curr Alzheimer Res , vol.6 , pp. 171-178
    • Sarasa, M.1    Pesini, P.2
  • 11
    • 38449121762 scopus 로고    scopus 로고
    • Molecular and genomic data identify the closest living relative of primates
    • Janecka JE, Miller W, Pringle TH, et al. Molecular and genomic data identify the closest living relative of primates. Science 2007;318:792-4.
    • (2007) Science , vol.318 , pp. 792-794
    • Janecka, J.E.1    Miller, W.2    Pringle, T.H.3
  • 12
    • 78651322166 scopus 로고    scopus 로고
    • Amyloid beta (Abeta) protein- and amyloid precursor protein (APP)- immunoreactive structures in the brains of aged tree shrews
    • Yamashita A, Fuchs E, Taira M, et al. Amyloid beta (Abeta) protein- and amyloid precursor protein (APP)- immunoreactive structures in the brains of aged tree shrews. Curr Aging Sci 2010;3:230-8.
    • (2010) Curr Aging Sci , vol.3 , pp. 230-238
    • Yamashita, A.1    Fuchs, E.2    Taira, M.3
  • 13
    • 77954507297 scopus 로고    scopus 로고
    • Amyloid-beta peptide and oligomers in the brain and cerebrospinal fluid of aged canines
    • Head E, Pop V, Sarsoza F, et al. Amyloid-beta peptide and oligomers in the brain and cerebrospinal fluid of aged canines. J Alzheimers Dis 2010;20:637-46.
    • (2010) J Alzheimers Dis , vol.20 , pp. 637-646
    • Head, E.1    Pop, V.2    Sarsoza, F.3
  • 14
    • 43649096717 scopus 로고    scopus 로고
    • A two-year study with fibrillar beta-amyloid (Abeta) immunization in aged canines: Effects on cognitive function and brain Abeta
    • Head E, Pop V, Vasilevko V, et al. A two-year study with fibrillar beta-amyloid (Abeta) immunization in aged canines: effects on cognitive function and brain Abeta. J Neurosci 2008;28:3555-66.
    • (2008) J Neurosci , vol.28 , pp. 3555-3566
    • Head, E.1    Pop, V.2    Vasilevko, V.3
  • 15
    • 0035678441 scopus 로고    scopus 로고
    • Effect of age and level of cognitive function on spontaneous and exploratory behaviors in the beagle dog
    • Siwak CT, Tapp PD, Milgram NW. Effect of age and level of cognitive function on spontaneous and exploratory behaviors in the beagle dog. Learn Mem 2001;8:317-25.
    • (2001) Learn Mem , vol.8 , pp. 317-325
    • Siwak, C.T.1    Tapp, P.D.2    Milgram, N.W.3
  • 16
    • 15744402275 scopus 로고    scopus 로고
    • Chronic antioxidant and mitochondrial cofactor administration improves discrimination learning in aged but not young dogs
    • Siwak CT, Tapp PD, Head E, et al. Chronic antioxidant and mitochondrial cofactor administration improves discrimination learning in aged but not young dogs. Prog Neuropsychopharmacol Biol Psychiatry 2005;29:461-9.
    • (2005) Prog Neuropsychopharmacol Biol Psychiatry , vol.29 , pp. 461-469
    • Siwak, C.T.1    Tapp, P.D.2    Head, E.3
  • 17
    • 15744391918 scopus 로고    scopus 로고
    • Therapeutic agents for the treatment of cognitive dysfunction syndrome in senior dogs
    • Landsberg G. Therapeutic agents for the treatment of cognitive dysfunction syndrome in senior dogs. Prog Neuropsychopharmacol Biol Psychiatry 2005;29:471-9.
    • (2005) Prog Neuropsychopharmacol Biol Psychiatry , vol.29 , pp. 471-479
    • Landsberg, G.1
  • 18
    • 0033768490 scopus 로고    scopus 로고
    • Comparison of the effects of adrafinil, propentofylline, and nicergoline on behavior in aged dogs
    • Siwak CT, Gruet P, Woehrle F, et al. Comparison of the effects of adrafinil, propentofylline, and nicergoline on behavior in aged dogs. Am J Vet Res 2000;61:1410-4.
    • (2000) Am J Vet Res , vol.61 , pp. 1410-1414
    • Siwak, C.T.1    Gruet, P.2    Woehrle, F.3
  • 19
    • 23944510149 scopus 로고    scopus 로고
    • The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing
    • Carrodeguas JA, Rodolosse A, Garza MV, et al. The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing. Neuroscience 2005;134:1285-300.
    • (2005) Neuroscience , vol.134 , pp. 1285-1300
    • Carrodeguas, J.A.1    Rodolosse, A.2    Garza, M.V.3
  • 20
    • 46849101764 scopus 로고    scopus 로고
    • Metal concentrations in plasma and cerebrospinal fluid in patients with Alzheimer's disease
    • Gerhardsson L, Lundh T, Minthon L, et al. Metal concentrations in plasma and cerebrospinal fluid in patients with Alzheimer's disease. Dement Geriatr Cogn Disord 2008;25:508-15.
    • (2008) Dement Geriatr Cogn Disord , vol.25 , pp. 508-515
    • Gerhardsson, L.1    Lundh, T.2    Minthon, L.3
  • 21
    • 33845938544 scopus 로고    scopus 로고
    • A longitudinal study of rats chronically exposed to aluminum at human dietary levels
    • Walton JR. A longitudinal study of rats chronically exposed to aluminum at human dietary levels. Neurosci Lett 2007;412:29-33.
    • (2007) Neurosci Lett , vol.412 , pp. 29-33
    • Walton, J.R.1
  • 22
    • 60849096351 scopus 로고    scopus 로고
    • Altered expression of Abeta metabolism-associated molecules from D-galactose/AlCl(3) induced mouse brain
    • Luo Y, Niu F, Sun Z, et al. Altered expression of Abeta metabolism-associated molecules from D-galactose/AlCl(3) induced mouse brain. Mech Ageing Dev 2009;130:248-52.
    • (2009) Mech Ageing Dev , vol.130 , pp. 248-252
    • Luo, Y.1    Niu, F.2    Sun, Z.3
  • 23
    • 64049117227 scopus 로고    scopus 로고
    • Protective effects of gastrodia elata on aluminium-chloride-induced learning impairments and alterations of amino acid neurotransmitter release in adult rats
    • Shuchang H, Qiao N, Piye N, et al. Protective effects of gastrodia elata on aluminium-chloride-induced learning impairments and alterations of amino acid neurotransmitter release in adult rats. Restor Neurol Neurosci 2008;26:467-73.
    • (2008) Restor Neurol Neurosci , vol.26 , pp. 467-473
    • Shuchang, H.1    Qiao, N.2    Piye, N.3
  • 24
    • 84865374076 scopus 로고    scopus 로고
    • Locomotor activity and learning and memory abilities in Alzheimer's disease induced by Aluminum in an acid environment in Zebrafish
    • He X, Zhong ZM, Che Y. [Locomotor activity and learning and memory abilities in Alzheimer's disease induced by Aluminum in an acid environment in Zebrafish].Dongwuxue Yanjiu 2012;33:231-6.
    • (2012) Dongwuxue Yanjiu , vol.33 , pp. 231-236
    • He, X.1    Zhong, Z.M.2    Che, Y.3
  • 25
    • 80052779276 scopus 로고    scopus 로고
    • Toxicity of Alzheimer's disease-associated Abeta peptide is ameliorated in a Drosophila model by tight control of zinc and copper availability
    • Hua H, Munter L, Harmeier A, et al. Toxicity of Alzheimer's disease-associated Abeta peptide is ameliorated in a Drosophila model by tight control of zinc and copper availability. Biol Chem 2011;392:919-26.
    • (2011) Biol Chem , vol.392 , pp. 919-926
    • Hua, H.1    Munter, L.2    Harmeier, A.3
  • 26
    • 23944449576 scopus 로고    scopus 로고
    • Brain aluminum, magnesium and phosphorus contents of control and Alzheimerdiseased patients
    • Andrasi E, Pali N, Molnar Z, et al. Brain aluminum, magnesium and phosphorus contents of control and Alzheimerdiseased patients. J Alzheimers Dis 2005;7:273-84.
    • (2005) J Alzheimers Dis , vol.7 , pp. 273-284
    • Andrasi, E.1    Pali, N.2    Molnar, Z.3
  • 27
    • 79959613455 scopus 로고    scopus 로고
    • Copper ions influence the toxicity of beta-amyloid(1-42) in a concentration-dependent manner in a Caenorhabditis elegans model of Alzheimer's disease
    • Luo Y, Zhang J, Liu N, et al. Copper ions influence the toxicity of beta-amyloid(1-42) in a concentration-dependent manner in a Caenorhabditis elegans model of Alzheimer's disease. Sci China Life Sci 2011;54:527-34.
    • (2011) Sci China Life Sci , vol.54 , pp. 527-534
    • Luo, Y.1    Zhang, J.2    Liu, N.3
  • 28
    • 67749114631 scopus 로고    scopus 로고
    • Midlife serum cholesterol and increased risk of Alzheimer's and vascular dementia three decades later
    • Solomon A, Kivipelto M, Wolozin B, et al. Midlife serum cholesterol and increased risk of Alzheimer's and vascular dementia three decades later. Dement Geriatr Cogn Disord 2009;28:75-80.
    • (2009) Dement Geriatr Cogn Disord , vol.28 , pp. 75-80
    • Solomon, A.1    Kivipelto, M.2    Wolozin, B.3
  • 29
    • 0034098980 scopus 로고    scopus 로고
    • Alterations of Alzheimer's disease in the cholesterol-fed rabbit, including vascular inflammation
    • Sparks DL,Kuo YM, Roher A, et al. Alterations of Alzheimer's disease in the cholesterol-fed rabbit, including vascular inflammation. Preliminary observations. Ann N Y Acad Sci 2000;903:335-44.
    • (2000) Preliminary Observations. Ann N y Acad Sci , vol.903 , pp. 335-344
    • Sparks, D.L.1    Kuo, Y.M.2    Roher, A.3
  • 30
    • 84861525034 scopus 로고    scopus 로고
    • Deferiprone reduces amyloid-beta and tau phosphorylation levels but not reactive oxygen species generation in hippocampus of rabbits fed a cholesterol-enriched diet
    • Prasanthi JR, Schrag M, Dasari B, et al. Deferiprone reduces amyloid-beta and tau phosphorylation levels but not reactive oxygen species generation in hippocampus of rabbits fed a cholesterol-enriched diet. J Alzheimers Dis 2012;30:167-82.
    • (2012) J Alzheimers Dis , vol.30 , pp. 167-182
    • Prasanthi, J.R.1    Schrag, M.2    Dasari, B.3
  • 31
    • 33746929523 scopus 로고    scopus 로고
    • Chronic systemic D-galactose exposure induces memory loss, neurodegeneration, and oxidative damage in mice: Protective effects of R-alpha-lipoic acid
    • Cui X, Zuo P, Zhang Q, et al. Chronic systemic D-galactose exposure induces memory loss, neurodegeneration, and oxidative damage in mice: protective effects of R-alpha-lipoic acid. J Neurosci Res 2006;84:647-54.
    • (2006) J Neurosci Res , vol.84 , pp. 647-654
    • Cui, X.1    Zuo, P.2    Zhang, Q.3
  • 32
    • 34147101836 scopus 로고    scopus 로고
    • Long-term D-galactose injection combined with ovariectomy serves as a new rodent model for Alzheimer's disease
    • Hua X, Lei M, Zhang Y, et al. Long-term D-galactose injection combined with ovariectomy serves as a new rodent model for Alzheimer's disease. Life Sci 2007;80:1897-905.
    • (2007) Life Sci , vol.80 , pp. 1897-1905
    • Hua, X.1    Lei, M.2    Zhang, Y.3
  • 33
    • 75949108679 scopus 로고    scopus 로고
    • Alteration of Abeta metabolism-related molecules in predementia induced by AlCl3 and D-galactose
    • Sun ZZ, Chen ZB, Jiang H, et al. Alteration of Abeta metabolism-related molecules in predementia induced by AlCl3 and D-galactose. Age (Dordr) 2009;31:277-84.
    • (2009) Age (Dordr) , vol.31 , pp. 277-284
    • Sun, Z.Z.1    Chen, Z.B.2    Jiang, H.3
  • 34
    • 34249030519 scopus 로고    scopus 로고
    • Neprilysin protects neurons against Abeta peptide toxicity
    • El-Amouri SS, Zhu H, Yu J, et al. Neprilysin protects neurons against Abeta peptide toxicity. Brain Res 2007;1152:191-200.
    • (2007) Brain Res , vol.1152 , pp. 191-200
    • El-Amouri, S.S.1    Zhu, H.2    Yu, J.3
  • 35
    • 0028177692 scopus 로고
    • Beta-Amyloid proteininduced Alzheimer's disease animal model
    • Nitta A, Itoh A, Hasegawa T, et al. beta-Amyloid proteininduced Alzheimer's disease animal model. Neurosci Lett 1994;170:63-6.
    • (1994) Neurosci Lett , vol.170 , pp. 63-66
    • Nitta, A.1    Itoh, A.2    Hasegawa, T.3
  • 36
    • 79959909169 scopus 로고    scopus 로고
    • Neuropathological changes in brain cortex and hippocampus in a rat model of Alzheimer's disease
    • NobakhtM, Hoseini SM,Mortazavi P, et al. Neuropathological changes in brain cortex and hippocampus in a rat model of Alzheimer's disease. Iran Biomed J 2011;15:51-8.
    • (2011) Iran Biomed J , vol.15 , pp. 51-58
    • Nobakht, M.1    Hoseini, S.M.2    Mortazavi, P.3
  • 37
    • 78149406228 scopus 로고    scopus 로고
    • A nonhuman primate model of Alzheimer's disease generated by intracranial injection of amyloid-beta42 and thiorphan
    • Li W, Wu Y, Min F, et al. A nonhuman primate model of Alzheimer's disease generated by intracranial injection of amyloid-beta42 and thiorphan. Metab Brain Dis 2010;25:277-84.
    • (2010) Metab Brain Dis , vol.25 , pp. 277-284
    • Li, W.1    Wu, Y.2    Min, F.3
  • 38
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings LM, Oddo S, Green KN, et al. Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 2005;45:675-88.
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3
  • 39
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991;349:704-6.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 40
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell J, Farlow M, Ghetti B, et al. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 1991;254:97-9.
    • (1991) Science , vol.254 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3
  • 41
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • Mullan M, Crawford F, Axelman K, et al. A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nat Genet 1992;1:345-7.
    • (1992) Nat Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 42
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 1996;274:99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 43
    • 0033525520 scopus 로고    scopus 로고
    • Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain
    • Moechars D, Dewachter I, Lorent K, et al. Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain. J Biol Chem 1999;274:6483-92.
    • (1999) J Biol Chem , vol.274 , pp. 6483-6492
    • Moechars, D.1    Dewachter, I.2    Lorent, K.3
  • 44
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999;400:173-7.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 45
    • 3042839092 scopus 로고    scopus 로고
    • Passive amyloid immunotherapy clears amyloid and transiently activates microglia in a transgenic mouse model of amyloid deposition
    • Wilcock DM, Rojiani A, Rosenthal A, et al. Passive amyloid immunotherapy clears amyloid and transiently activates microglia in a transgenic mouse model of amyloid deposition. J Neurosci 2004;24:6144-51.
    • (2004) J Neurosci , vol.24 , pp. 6144-6151
    • Wilcock, D.M.1    Rojiani, A.2    Rosenthal, A.3
  • 46
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, et al. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 2000;6:916-9.
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3
  • 47
    • 80051544073 scopus 로고    scopus 로고
    • Animal models in the drug discovery pipeline for Alzheimer's disease
    • Van Dam D, De Deyn PP. Animal models in the drug discovery pipeline for Alzheimer's disease. Br J Pharmacol 2011;164:1285-300.
    • (2011) Br J Pharmacol , vol.164 , pp. 1285-1300
    • Van Dam, D.1    De Deyn, P.P.2
  • 48
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • Citron M, Westaway D, Xia W, et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat Med 1997;3:67-72.
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 49
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • Chui DH, Tanahashi H, Ozawa K, et al. Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nat Med 1999;5:560-4.
    • (1999) Nat Med , vol.5 , pp. 560-564
    • Chui, D.H.1    Tanahashi, H.2    Ozawa, K.3
  • 50
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloidbeta42( 43) in brains of mice expressing mutant presenilin 1
    • Duff K, Eckman C, Zehr C, et al. Increased amyloidbeta42( 43) in brains of mice expressing mutant presenilin 1. Nature 1996;383:710-3.
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 51
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb L, Gordon MN, McGowan E, et al. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat Med 1998;4:97-100.
    • (1998) Nat Med , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3
  • 52
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • Borchelt DR, Ratovitski T, van Lare J, et al. Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 1997;19:939-45.
    • (1997) Neuron , vol.19 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    Van Lare, J.3
  • 53
    • 84874954551 scopus 로고    scopus 로고
    • Quetiapine modulates conditioned anxiety and alternation behavior in Alzheimer's transgenic mice
    • Feb
    • Tempier A, He J, Zhu S, et al. Quetiapine modulates conditioned anxiety and alternation behavior in Alzheimer's transgenic mice. Curr Alzheimer Res. 2013 Feb;10(2):199-206.
    • (2013) Curr Alzheimer Res. , vol.10 , Issue.2 , pp. 199-206
    • Tempier, A.1    He, J.2    Zhu, S.3
  • 54
    • 60249088016 scopus 로고    scopus 로고
    • Cryptotanshinone, a compound from Salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates beta-amyloid deposition through upregulating alpha-secretase in vivo and in vitro
    • Mei Z, Zhang F, Tao L, et al. Cryptotanshinone, a compound from Salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates beta-amyloid deposition through upregulating alpha-secretase in vivo and in vitro. Neurosci Lett 2009;452:90-5.
    • (2009) Neurosci Lett , vol.452 , pp. 90-95
    • Mei, Z.1    Zhang, F.2    Tao, L.3
  • 55
    • 77950377674 scopus 로고    scopus 로고
    • Reduction of betaamyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease
    • Paris D, Ganey NJ, Laporte V, et al. Reduction of betaamyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease. J Neuroinflammation 2010;7:17.
    • (2010) J Neuroinflammation , vol.7 , pp. 17
    • Paris, D.1    Ganey, N.J.2    Laporte, V.3
  • 56
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo S, Caccamo A, Kitazawa M, et al. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease.Neurobiol Aging 2003;24:1063- 70.
    • (2003) Neurobiol Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3
  • 58
    • 79952528559 scopus 로고    scopus 로고
    • Apomorphine treatment in Alzheimer mice promoting amyloid-beta degradation
    • Himeno E, Ohyagi Y, Ma L, et al. Apomorphine treatment in Alzheimer mice promoting amyloid-beta degradation. Ann Neurol 2011;69:248-56.
    • (2011) Ann Neurol , vol.69 , pp. 248-256
    • Himeno, E.1    Ohyagi, Y.2    Ma, L.3
  • 59
    • 84860439512 scopus 로고    scopus 로고
    • Dantrolene ameliorates cognitive decline and neuropathology in Alzheimer triple transgenic mice
    • Peng J, Liang G, Inan S, et al. Dantrolene ameliorates cognitive decline and neuropathology in Alzheimer triple transgenic mice. Neurosci Lett 2012;516:274-9.
    • (2012) Neurosci Lett , vol.516 , pp. 274-279
    • Peng, J.1    Liang, G.2    Inan, S.3
  • 60
    • 33846068454 scopus 로고    scopus 로고
    • WormBook: The online review of Caenorhabditis elegans biology
    • Girard LR, Fiedler TJ, Harris TW, et al. WormBook: the online review of Caenorhabditis elegans biology. Nucleic Acids Res 2007;35:D472-5.
    • (2007) Nucleic Acids Res , vol.35
    • Girard, L.R.1    Fiedler, T.J.2    Harris, T.W.3
  • 61
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • Link CD. Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc Natl Acad Sci U S A 1995;92:9368-72.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 62
    • 0031712488 scopus 로고    scopus 로고
    • In vivo aggregation of betaamyloid peptide variants
    • Fay DS, Fluet A, Johnson CJ, et al. In vivo aggregation of betaamyloid peptide variants. J Neurochem 1998;71:1616-25.
    • (1998) J Neurochem , vol.71 , pp. 1616-1625
    • Fay, D.S.1    Fluet, A.2    Johnson, C.J.3
  • 63
    • 0035109444 scopus 로고    scopus 로고
    • Visualization of fibrillar amyloid deposits in living, transgenic Caenorhabditis elegans animals using the sensitive amyloid dye, X-34
    • Link CD, Johnson CJ, Fonte V, et al. Visualization of fibrillar amyloid deposits in living, transgenic Caenorhabditis elegans animals using the sensitive amyloid dye, X-34. Neurobiol Aging 2001;22:217-26.
    • (2001) Neurobiol Aging , vol.22 , pp. 217-226
    • Link, C.D.1    Johnson, C.J.2    Fonte, V.3
  • 64
    • 0033857342 scopus 로고    scopus 로고
    • X-34, a fluorescent derivative of Congo red: A novel histochemical stain for Alzheimer's disease pathology
    • Styren SD, Hamilton RL, Styren GC, et al. X-34, a fluorescent derivative of Congo red: a novel histochemical stain for Alzheimer's disease pathology. J Histochem Cytochem 2000;48:1223-32.
    • (2000) J Histochem Cytochem , vol.48 , pp. 1223-1232
    • Styren, S.D.1    Hamilton, R.L.2    Styren, G.C.3
  • 65
    • 0032616381 scopus 로고    scopus 로고
    • Transgenic zebrafish
    • Jowett T. Transgenic zebrafish. Methods Mol Biol 1999;97:461-86.
    • (1999) Methods Mol Biol , vol.97 , pp. 461-486
    • Jowett, T.1
  • 66
    • 77950457762 scopus 로고    scopus 로고
    • Transgenic zebrafish models of neurodegenerative diseases
    • Sager JJ, Bai Q, Burton EA. Transgenic zebrafish models of neurodegenerative diseases. Brain Struct Funct 2010;214:285-302.
    • (2010) Brain Struct Funct , vol.214 , pp. 285-302
    • Sager, J.J.1    Bai, Q.2    Burton, E.A.3
  • 67
    • 78751705313 scopus 로고    scopus 로고
    • Zebrafish as a tool in Alzheimer's disease research
    • Newman M, Verdile G, Martins RN, et al. Zebrafish as a tool in Alzheimer's disease research. Biochim Biophys Acta 2011;1812:346-52.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 346-352
    • Newman, M.1    Verdile, G.2    Martins, R.N.3
  • 68
    • 77953627393 scopus 로고    scopus 로고
    • A zebrafish melanophore model of amyloid beta toxicity
    • Newman M, Wilson L, Camp E, et al. A zebrafish melanophore model of amyloid beta toxicity. Zebrafish 2010;7:155-9.
    • (2010) Zebrafish , vol.7 , pp. 155-159
    • Newman, M.1    Wilson, L.2    Camp, E.3
  • 70
    • 36148960495 scopus 로고    scopus 로고
    • Generation of a transgenic zebrafish model of Tauopathy using a novel promoter element derived from the zebrafish eno2 gene
    • Bai Q, Garver JA, Hukriede NA, et al. Generation of a transgenic zebrafish model of Tauopathy using a novel promoter element derived from the zebrafish eno2 gene. Nucleic Acids Res 2007;35:6501-16.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6501-6516
    • Bai, Q.1    Garver, J.A.2    Hukriede, N.A.3
  • 71
    • 66449115032 scopus 로고    scopus 로고
    • A zebrafishmodel of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation
    • Paquet D, Bhat R, Sydow A, et al. A zebrafishmodel of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation. J Clin Invest 2009;119:1382-95.
    • (2009) J Clin Invest , vol.119 , pp. 1382-1395
    • Paquet, D.1    Bhat, R.2    Sydow, A.3
  • 72
    • 61449261803 scopus 로고    scopus 로고
    • Drosophila melanogaster as a model organism of brain diseases
    • Jeibmann A, Paulus W. Drosophila melanogaster as a model organism of brain diseases. Int J Mol Sci 2009;10:407-40.
    • (2009) Int J Mol Sci , vol.10 , pp. 407-440
    • Jeibmann, A.1    Paulus, W.2
  • 73
    • 2142645114 scopus 로고    scopus 로고
    • Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila
    • Greeve I, Kretzschmar D, Tschape JA, et al. Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila. J Neurosci 2004;24:3899-906.
    • (2004) J Neurosci , vol.24 , pp. 3899-3906
    • Greeve, I.1    Kretzschmar, D.2    Tschape, J.A.3
  • 74
    • 3242809725 scopus 로고    scopus 로고
    • A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster
    • Finelli A, Kelkar A, Song HJ, et al. A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster. Mol Cell Neurosci 2004;26:365-75.
    • (2004) Mol Cell Neurosci , vol.26 , pp. 365-375
    • Finelli, A.1    Kelkar, A.2    Song, H.J.3
  • 75
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • Crowther DC, Kinghorn KJ, Miranda E, et al. Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease. Neuroscience 2005;132:123-35.
    • (2005) Neuroscience , vol.132 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3
  • 76
    • 45949102576 scopus 로고    scopus 로고
    • Abeta42 mutants with different aggregation profiles induce distinct pathologies in Drosophila
    • Iijima K, Chiang HC, Hearn SA, et al. Abeta42 mutants with different aggregation profiles induce distinct pathologies in Drosophila. PLoS One 2008;3:e1703.
    • (2008) PLoS One , vol.3
    • Iijima, K.1    Chiang, H.C.2    Hearn, S.A.3
  • 77
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman JM, Feany MB. Genetic modifiers of tauopathy in Drosophila. Genetics 2003;165:1233-42.
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 78
    • 0037118247 scopus 로고    scopus 로고
    • Human wildtype tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson GR, Wiedau-Pazos M, Sang TK, et al. Human wildtype tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 2002;34:509-19.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3
  • 79
    • 77952148678 scopus 로고    scopus 로고
    • Ascidians: An invertebrate chordate model to study Alzheimer's disease pathogenesis
    • Virata MJ, Zeller RW. Ascidians: an invertebrate chordate model to study Alzheimer's disease pathogenesis. Dis Model Mech 2010;3:377-85.
    • (2010) Dis Model Mech , vol.3 , pp. 377-385
    • Virata, M.J.1    Zeller, R.W.2
  • 80
    • 33847133125 scopus 로고    scopus 로고
    • Targeting soluble Abeta peptide with Tramiprosate for the treatment of brain amyloidosis
    • Gervais F, Paquette J, Morissette C, et al. Targeting soluble Abeta peptide with Tramiprosate for the treatment of brain amyloidosis. Neurobiol Aging 2007;28:537-47.
    • (2007) Neurobiol Aging , vol.28 , pp. 537-547
    • Gervais, F.1    Paquette, J.2    Morissette, C.3
  • 81
    • 78349236925 scopus 로고    scopus 로고
    • Yeast as a model for studying Alzheimer's disease
    • Bharadwaj P, Martins R, Macreadie I. Yeast as a model for studying Alzheimer's disease. FEMS Yeast Res 2010;10:961-9.
    • (2010) FEMS Yeast Res , vol.10 , pp. 961-969
    • Bharadwaj, P.1    Martins, R.2    Macreadie, I.3
  • 82
    • 0028072316 scopus 로고
    • Proteolytic processing and secretion of human beta-amyloid precursor protein in yeast. Evidence for a yeast secretase activity
    • Zhang H, Komano H, Fuller RS, et al. Proteolytic processing and secretion of human beta-amyloid precursor protein in yeast. Evidence for a yeast secretase activity. J Biol Chem 1994;269:27799-802.
    • (1994) J Biol Chem , vol.269 , pp. 27799-27802
    • Zhang, H.1    Komano, H.2    Fuller, R.S.3
  • 83
    • 0032553018 scopus 로고    scopus 로고
    • Processing of the Alzheimer's disease amyloid precursor protein in Pichia pastoris: Immunodetection of alpha-, beta-, and gamma-secretase products
    • Le Brocque D, Henry A, Cappai R, et al. Processing of the Alzheimer's disease amyloid precursor protein in Pichia pastoris: immunodetection of alpha-, beta-, and gamma-secretase products. Biochemistry 1998;37:14958-65.
    • (1998) Biochemistry , vol.37 , pp. 14958-14965
    • Le Brocque, D.1    Henry, A.2    Cappai, R.3
  • 84
    • 0030700930 scopus 로고    scopus 로고
    • Characterization of betaamyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases
    • ZhangW, EspinozaD,Hines V, et al. Characterization of betaamyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases. Biochim Biophys Acta 1997;1359:110-22.
    • (1997) Biochim Biophys Acta , vol.1359 , pp. 110-122
    • Zhang, W.1    Espinoza, D.2    Hines, V.3
  • 85
    • 0037451709 scopus 로고    scopus 로고
    • Human beta-secretase activity in yeast detected by a novel cellular growth selection system
    • Luthi U, Schaerer-Brodbeck C, Tanner S, et al. Human beta-secretase activity in yeast detected by a novel cellular growth selection system. Biochim Biophys Acta 2003;1620: 167-78.
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 167-178
    • Luthi, U.1    Schaerer-Brodbeck, C.2    Tanner, S.3
  • 86
    • 4444330269 scopus 로고    scopus 로고
    • Yeast growth selection system for the identification of cell-active inhibitors of beta-secretase
    • Middendorp O, Ortler C, Neumann U, et al. Yeast growth selection system for the identification of cell-active inhibitors of beta-secretase. Biochim Biophys Acta 2004;1674:29-39.
    • (2004) Biochim Biophys Acta , vol.1674 , pp. 29-39
    • Middendorp, O.1    Ortler, C.2    Neumann, U.3
  • 87
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of gamma-secretase activity
    • Edbauer D, Winkler E, Regula JT, et al. Reconstitution of gamma-secretase activity. Nat Cell Biol 2003;5:486-8.
    • (2003) Nat Cell Biol , vol.5 , pp. 486-488
    • Edbauer, D.1    Winkler, E.2    Regula, J.T.3
  • 88
    • 4444221162 scopus 로고    scopus 로고
    • Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1
    • Edbauer D, Kaether C, Steiner H, et al. Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1. J Biol Chem 2004;279:37311-15.
    • (2004) J Biol Chem , vol.279 , pp. 37311-37315
    • Edbauer, D.1    Kaether, C.2    Steiner, H.3
  • 89
    • 66349111071 scopus 로고    scopus 로고
    • Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations
    • Futai E, Yagishita S, Ishiura S. Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations. J Biol Chem 2009;284:13013-22.
    • (2009) J Biol Chem , vol.284 , pp. 13013-13022
    • Futai, E.1    Yagishita, S.2    Ishiura, S.3
  • 90
    • 0033452916 scopus 로고    scopus 로고
    • An in vivo assay for the identification of target proteases which cleave membrane-associated substrates
    • Steiner H, Pesold B, Haass C. An in vivo assay for the identification of target proteases which cleave membrane-associated substrates. FEBS Lett 1999;463:245-9.
    • (1999) FEBS Lett , vol.463 , pp. 245-249
    • Steiner, H.1    Pesold, B.2    Haass, C.3
  • 91
    • 0035831499 scopus 로고    scopus 로고
    • A pathogenic presenilin-1 deletion causes abberrant Abeta 42 production in the absence of congophilic amyloid plaques
    • Steiner H, Revesz T, Neumann M, et al. A pathogenic presenilin-1 deletion causes abberrant Abeta 42 production in the absence of congophilic amyloid plaques. J Biol Chem 2001;276:7233-9.
    • (2001) J Biol Chem , vol.276 , pp. 7233-7239
    • Steiner, H.1    Revesz, T.2    Neumann, M.3
  • 92
    • 0029872929 scopus 로고    scopus 로고
    • Two-hybrid system as a model to study the interaction of beta-amyloid peptide monomers
    • Hughes SR, Goyal S, Sun JE, et al. Two-hybrid system as a model to study the interaction of beta-amyloid peptide monomers. Proc Natl Acad Sci U S A 1996;93:2065-70.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 2065-2070
    • Hughes, S.R.1    Goyal, S.2    Sun, J.E.3
  • 93
    • 35448944853 scopus 로고    scopus 로고
    • Alzheimer's Abeta fused to green fluorescent protein induces growth stress and a heat shock response
    • Caine J, Sankovich S, AntonyH, et al. Alzheimer's Abeta fused to green fluorescent protein induces growth stress and a heat shock response. FEMS Yeast Res 2007;7:1230-6.
    • (2007) FEMS Yeast Res , vol.7 , pp. 1230-1236
    • Caine, J.1    Sankovich, S.2    Antony, H.3
  • 94
    • 57349160497 scopus 로고    scopus 로고
    • Validation of folate in a convenient yeast assay suited for identification of inhibitors of Alzheimer's amyloid-beta aggregation
    • Macreadie I, Lotfi-Miri M, Mohotti S, et al. Validation of folate in a convenient yeast assay suited for identification of inhibitors of Alzheimer's amyloid-beta aggregation. J Alzheimers Dis 2008;15:391-6.
    • (2008) J Alzheimers Dis , vol.15 , pp. 391-396
    • Macreadie, I.1    Lotfi-Miri, M.2    Mohotti, S.3
  • 95
    • 23944469853 scopus 로고    scopus 로고
    • Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast
    • Vandebroek T, Vanhelmont T, Terwel D, et al. Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 2005;44:11466-75.
    • (2005) Biochemistry , vol.44 , pp. 11466-11475
    • Vandebroek, T.1    Vanhelmont, T.2    Terwel, D.3
  • 96
    • 33748746596 scopus 로고    scopus 로고
    • Microtubule binding and clustering of human Tau-4R and Tau- P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5
    • Vandebroek T, Terwel D, Vanhelmont T, et al. Microtubule binding and clustering of human Tau-4R and Tau- P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5. J Biol Chem 2006;281:25388-97.
    • (2006) J Biol Chem , vol.281 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3
  • 97
    • 44849144494 scopus 로고    scopus 로고
    • A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast
    • Bharadwaj P, Waddington L, Varghese J, et al. A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast. J Alzheimers Dis 2008;13:147-50.
    • (2008) J Alzheimers Dis , vol.13 , pp. 147-150
    • Bharadwaj, P.1    Waddington, L.2    Varghese, J.3
  • 98
    • 3142655729 scopus 로고    scopus 로고
    • Transgenic animal models of Alzheimer's disease and related disorders: Histopathology, behavior and therapy
    • Gotz J, Streffer JR, David D, et al. Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy. Mol Psychiatry 2004;9:664-83.
    • (2004) Mol Psychiatry , vol.9 , pp. 664-683
    • Gotz, J.1    Streffer, J.R.2    David, D.3
  • 99
    • 11344294035 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease: How useful have they been for therapeutic development?
    • Duff K, Suleman F. Transgenic mouse models of Alzheimer's disease: how useful have they been for therapeutic development? Brief Funct Genomic Proteomic 2004;3:47-59.
    • (2004) Brief Funct Genomic Proteomic , vol.3 , pp. 47-59
    • Duff, K.1    Suleman, F.2
  • 100
    • 84861480990 scopus 로고    scopus 로고
    • Somatostatinimmunoreactive senile plaque-like structures in the frontal cortex and nucleus accumbens of aged tree shrews and Japanese macaques
    • Yamashita A, Fuchs E, Taira M, et al. Somatostatinimmunoreactive senile plaque-like structures in the frontal cortex and nucleus accumbens of aged tree shrews and Japanese macaques. J Med Primatol 2012;41:147-57.
    • (2012) J Med Primatol , vol.41 , pp. 147-157
    • Yamashita, A.1    Fuchs, E.2    Taira, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.