메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

A Powerful Yeast Model to Investigate the Synergistic Interaction of α-Synuclein and Tau in Neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; GLYCOGEN SYNTHASE KINASE 3BETA; ISOPROTEIN; MUTANT PROTEIN; PROTEIN SERINE THREONINE KINASE; SERINE; TAU PROTEIN;

EID: 84873517075     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055848     Document Type: Article
Times cited : (28)

References (74)
  • 1
    • 34248595601 scopus 로고    scopus 로고
    • alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
    • Esposito A, Dohm CP, Kermer P, Bahr M, Wouters FS, (2007) alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton. Neurobiol Dis 26: 521-531.
    • (2007) Neurobiol Dis , vol.26 , pp. 521-531
    • Esposito, A.1    Dohm, C.P.2    Kermer, P.3    Bahr, M.4    Wouters, F.S.5
  • 2
    • 10044281817 scopus 로고    scopus 로고
    • Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with tau-based inclusions
    • Popescu A, Lippa CF, Lee VM, Trojanowski JQ, (2004) Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with tau-based inclusions. Arch Neurol 61: 1915-1919.
    • (2004) Arch Neurol , vol.61 , pp. 1915-1919
    • Popescu, A.1    Lippa, C.F.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 3
    • 84857442897 scopus 로고    scopus 로고
    • SNCA and MAPT genes: Independent and joint effects in Parkinson disease in the Italian population
    • Trotta L, Guella I, Solda G, Sironi F, Tesei S, et al. (2012) SNCA and MAPT genes: Independent and joint effects in Parkinson disease in the Italian population. Parkinsonism Relat Disord 18: 257-262.
    • (2012) Parkinsonism Relat Disord , vol.18 , pp. 257-262
    • Trotta, L.1    Guella, I.2    Solda, G.3    Sironi, F.4    Tesei, S.5
  • 6
  • 7
  • 10
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, et al. (2004) Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364: 1167-1169.
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3    Mouroux, V.4    Douay, X.5
  • 12
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, et al. (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 18: 106-108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5
  • 13
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. (1997) Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276: 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 14
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia
    • Zarranz JJ, Alegre J, Gomez-Esteban JC, Lezcano E, Ros R, et al. (2004) The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 55: 164-173.
    • (2004) Ann Neurol , vol.55 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gomez-Esteban, J.C.3    Lezcano, E.4    Ros, R.5
  • 15
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ, (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 83: 4044-4048.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 16
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, et al. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261: 6084-6089.
    • (1986) J Biol Chem , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4    Zaidi, M.S.5
  • 19
    • 79960325654 scopus 로고    scopus 로고
    • The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics
    • Pritchard SM, Dolan PJ, Vitkus A, Johnson GV, (2011) The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics. J Cell Mol Med 15: 1621-1635.
    • (2011) J Cell Mol Med , vol.15 , pp. 1621-1635
    • Pritchard, S.M.1    Dolan, P.J.2    Vitkus, A.3    Johnson, G.V.4
  • 20
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W, (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 15: 112-119.
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 21
    • 78649660787 scopus 로고    scopus 로고
    • Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss
    • Kimura T, Fukuda T, Sahara N, Yamashita S, Murayama M, et al. (2010) Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss. J Biol Chem 285: 38692-38699.
    • (2010) J Biol Chem , vol.285 , pp. 38692-38699
    • Kimura, T.1    Fukuda, T.2    Sahara, N.3    Yamashita, S.4    Murayama, M.5
  • 22
    • 0034718203 scopus 로고    scopus 로고
    • Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease
    • Goedert M, Spillantini MG, (2000) Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease. Biochim Biophys Acta 1502: 110-121.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 110-121
    • Goedert, M.1    Spillantini, M.G.2
  • 23
    • 79955389000 scopus 로고    scopus 로고
    • Independent and joint effects of the MAPT and SNCA genes in Parkinson disease
    • Elbaz A, Ross OA, Ioannidis JP, Soto-Ortolaza AI, Moisan F, et al. (2011) Independent and joint effects of the MAPT and SNCA genes in Parkinson disease. Ann Neurol 69: 778-792.
    • (2011) Ann Neurol , vol.69 , pp. 778-792
    • Elbaz, A.1    Ross, O.A.2    Ioannidis, J.P.3    Soto-Ortolaza, A.I.4    Moisan, F.5
  • 24
    • 59249100854 scopus 로고    scopus 로고
    • Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease
    • Fujishiro H, Uchikado H, Arai T, Hasegawa M, Akiyama H, et al. (2009) Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease. Acta Neuropathol 117: 151-158.
    • (2009) Acta Neuropathol , vol.117 , pp. 151-158
    • Fujishiro, H.1    Uchikado, H.2    Arai, T.3    Hasegawa, M.4    Akiyama, H.5
  • 26
    • 41549154550 scopus 로고    scopus 로고
    • Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies
    • Muntane G, Dalfo E, Martinez A, Ferrer I, (2008) Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies. Neuroscience 152: 913-923.
    • (2008) Neuroscience , vol.152 , pp. 913-923
    • Muntane, G.1    Dalfo, E.2    Martinez, A.3    Ferrer, I.4
  • 27
    • 0037466656 scopus 로고    scopus 로고
    • Initiation and synergistic fibrillization of tau and alpha-synuclein
    • Giasson BI, Forman MS, Higuchi M, Golbe LI, Graves CL, et al. (2003) Initiation and synergistic fibrillization of tau and alpha-synuclein. Science 300: 636-640.
    • (2003) Science , vol.300 , pp. 636-640
    • Giasson, B.I.1    Forman, M.S.2    Higuchi, M.3    Golbe, L.I.4    Graves, C.L.5
  • 28
    • 22144442365 scopus 로고    scopus 로고
    • Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation
    • Benussi L, Ghidoni R, Paterlini A, Nicosia F, Alberici AC, et al. (2005) Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation. Exp Cell Res 308: 78-84.
    • (2005) Exp Cell Res , vol.308 , pp. 78-84
    • Benussi, L.1    Ghidoni, R.2    Paterlini, A.3    Nicosia, F.4    Alberici, A.C.5
  • 29
    • 0033520474 scopus 로고    scopus 로고
    • alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • Jensen PH, Hager H, Nielsen MS, Hojrup P, Gliemann J, et al. (1999) alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J Biol Chem 274: 25481-25489.
    • (1999) J Biol Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5
  • 30
    • 33845643466 scopus 로고    scopus 로고
    • Alpha-synuclein induces hyperphosphorylation of Tau in the MPTP model of parkinsonism
    • Duka T, Rusnak M, Drolet RE, Duka V, Wersinger C, et al. (2006) Alpha-synuclein induces hyperphosphorylation of Tau in the MPTP model of parkinsonism. FASEB J 20: 2302-2312.
    • (2006) FASEB J , vol.20 , pp. 2302-2312
    • Duka, T.1    Rusnak, M.2    Drolet, R.E.3    Duka, V.4    Wersinger, C.5
  • 31
    • 79957636327 scopus 로고    scopus 로고
    • Induction of intracellular tau aggregation is promoted by alpha-synuclein seeds and provides novel insights into the hyperphosphorylation of tau
    • Waxman EA, Giasson BI, (2011) Induction of intracellular tau aggregation is promoted by alpha-synuclein seeds and provides novel insights into the hyperphosphorylation of tau. J Neurosci 31: 7604-7618.
    • (2011) J Neurosci , vol.31 , pp. 7604-7618
    • Waxman, E.A.1    Giasson, B.I.2
  • 32
    • 14844311246 scopus 로고    scopus 로고
    • Tau phosphorylation increases in symptomatic mice overexpressing A30P alpha-synuclein
    • Frasier M, Walzer M, McCarthy L, Magnuson D, Lee JM, et al. (2005) Tau phosphorylation increases in symptomatic mice overexpressing A30P alpha-synuclein. Exp Neurol 192: 274-287.
    • (2005) Exp Neurol , vol.192 , pp. 274-287
    • Frasier, M.1    Walzer, M.2    McCarthy, L.3    Magnuson, D.4    Lee, J.M.5
  • 33
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, et al. (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316: 750-754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5
  • 34
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, et al. (2010) Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 142: 387-397.
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5
  • 35
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • Roberson ED, Halabisky B, Yoo JW, Yao J, Chin J, et al. (2011) Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. J Neurosci 31: 700-711.
    • (2011) J Neurosci , vol.31 , pp. 700-711
    • Roberson, E.D.1    Halabisky, B.2    Yoo, J.W.3    Yao, J.4    Chin, J.5
  • 36
    • 83655181921 scopus 로고    scopus 로고
    • Tau reduction does not prevent motor deficits in two mouse models of Parkinson's disease
    • Morris M, Koyama A, Masliah E, Mucke L, (2011) Tau reduction does not prevent motor deficits in two mouse models of Parkinson's disease. PLoS One 6: e29257.
    • (2011) PLoS One , vol.6
    • Morris, M.1    Koyama, A.2    Masliah, E.3    Mucke, L.4
  • 37
    • 77957377567 scopus 로고    scopus 로고
    • LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3ss
    • Lin CH, Tsai PI, Wu RM, Chien CT, (2010) LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3ss. J Neurosci 30: 13138-13149.
    • (2010) J Neurosci , vol.30 , pp. 13138-13149
    • Lin, C.H.1    Tsai, P.I.2    Wu, R.M.3    Chien, C.T.4
  • 40
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro TF, Lindquist S, (2003) Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302: 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 41
    • 31644443193 scopus 로고    scopus 로고
    • A yeast-based model of alpha-synucleinopathy identifies compounds with therapeutic potential
    • Griffioen G, Duhamel H, Van Damme N, Pellens K, Zabrocki P, et al. (2006) A yeast-based model of alpha-synucleinopathy identifies compounds with therapeutic potential. Biochim Biophys Acta 1762: 312-318.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 312-318
    • Griffioen, G.1    Duhamel, H.2    Van Damme, N.3    Pellens, K.4    Zabrocki, P.5
  • 42
    • 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, Gysemans M, Van Haesendonck C, et al. (2006) 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 281: 25388-25397.
    • (2006) J Biol Chem , vol.281 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3    Gysemans, M.4    Van Haesendonck, C.5
  • 43
    • 78349245542 scopus 로고    scopus 로고
    • Serine-409 phosphorylation and oxidative damage define aggregation of human protein tau in yeast
    • Vanhelmont T, Vandebroek T, De Vos A, Terwel D, Lemaire K, et al. (2010) Serine-409 phosphorylation and oxidative damage define aggregation of human protein tau in yeast. FEMS Yeast Res 10: 992-1005.
    • (2010) FEMS Yeast Res , vol.10 , pp. 992-1005
    • Vanhelmont, T.1    Vandebroek, T.2    De Vos, A.3    Terwel, D.4    Lemaire, K.5
  • 44
    • 15944378475 scopus 로고    scopus 로고
    • Characterization of alpha-synuclein aggregation and synergistic toxicity with protein tau in yeast
    • Zabrocki P, Pellens K, Vanhelmont T, Vandebroek T, Griffioen G, et al. (2005) Characterization of alpha-synuclein aggregation and synergistic toxicity with protein tau in yeast. FEBS J 272: 1386-1400.
    • (2005) FEBS J , vol.272 , pp. 1386-1400
    • Zabrocki, P.1    Pellens, K.2    Vanhelmont, T.3    Vandebroek, T.4    Griffioen, G.5
  • 45
    • 34047143174 scopus 로고    scopus 로고
    • Epistatic buffering of fitness loss in yeast double deletion strains
    • Jasnos L, Korona R, (2007) Epistatic buffering of fitness loss in yeast double deletion strains. Nat Genet 39: 550-554.
    • (2007) Nat Genet , vol.39 , pp. 550-554
    • Jasnos, L.1    Korona, R.2
  • 46
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A, (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168.
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 47
    • 2442507000 scopus 로고    scopus 로고
    • Affordable image analysis using NIH Image/ImageJ
    • Girish V, Vijayalakshmi A, (2004) Affordable image analysis using NIH Image/ImageJ. Indian J Cancer 41: 47.
    • (2004) Indian J Cancer , vol.41 , pp. 47
    • Girish, V.1    Vijayalakshmi, A.2
  • 48
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • Flower TR, Chesnokova LS, Froelich CA, Dixon C, Witt SN, (2005) Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J Mol Biol 351: 1081-1100.
    • (2005) J Mol Biol , vol.351 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3    Dixon, C.4    Witt, S.N.5
  • 49
    • 79953183632 scopus 로고    scopus 로고
    • Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy
    • Fushimi K, Long C, Jayaram N, Chen X, Li L, et al. (2011) Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy. Protein Cell 2: 141-149.
    • (2011) Protein Cell , vol.2 , pp. 141-149
    • Fushimi, K.1    Long, C.2    Jayaram, N.3    Chen, X.4    Li, L.5
  • 50
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 51
    • 0041825135 scopus 로고    scopus 로고
    • Analysis of yeast prion aggregates with amyloid-staining compound in vivo
    • Kimura Y, Koitabashi S, Fujita T, (2003) Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct Funct 28: 187-193.
    • (2003) Cell Struct Funct , vol.28 , pp. 187-193
    • Kimura, Y.1    Koitabashi, S.2    Fujita, T.3
  • 53
    • 33646197357 scopus 로고    scopus 로고
    • Clinical and biochemical correlates of insoluble alpha-synuclein in dementia with Lewy bodies
    • Klucken J, Ingelsson M, Shin Y, Irizarry MC, Hedley-Whyte ET, et al. (2006) Clinical and biochemical correlates of insoluble alpha-synuclein in dementia with Lewy bodies. Acta Neuropathol 111: 101-108.
    • (2006) Acta Neuropathol , vol.111 , pp. 101-108
    • Klucken, J.1    Ingelsson, M.2    Shin, Y.3    Irizarry, M.C.4    Hedley-Whyte, E.T.5
  • 54
    • 0142124410 scopus 로고    scopus 로고
    • Primary progressive aphasia as the initial manifestation of corticobasal degeneration and unusual tauopathies
    • Ferrer I, Hernandez I, Boada M, Llorente A, Rey MJ, et al. (2003) Primary progressive aphasia as the initial manifestation of corticobasal degeneration and unusual tauopathies. Acta Neuropathol 106: 419-435.
    • (2003) Acta Neuropathol , vol.106 , pp. 419-435
    • Ferrer, I.1    Hernandez, I.2    Boada, M.3    Llorente, A.4    Rey, M.J.5
  • 55
    • 79951819429 scopus 로고    scopus 로고
    • Accelerated human mutant tau aggregation by knocking out murine tau in a transgenic mouse model
    • Ando K, Leroy K, Heraud C, Yilmaz Z, Authelet M, et al. (2011) Accelerated human mutant tau aggregation by knocking out murine tau in a transgenic mouse model. Am J Pathol 178: 803-816.
    • (2011) Am J Pathol , vol.178 , pp. 803-816
    • Ando, K.1    Leroy, K.2    Heraud, C.3    Yilmaz, Z.4    Authelet, M.5
  • 56
    • 58149234447 scopus 로고    scopus 로고
    • Aggregates assembled from overexpression of wild-type alpha-synuclein are not toxic to human neuronal cells
    • Ko LW, Ko HH, Lin WL, Kulathingal JG, Yen SH, (2008) Aggregates assembled from overexpression of wild-type alpha-synuclein are not toxic to human neuronal cells. J Neuropathol Exp Neurol 67: 1084-1096.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 1084-1096
    • Ko, L.W.1    Ko, H.H.2    Lin, W.L.3    Kulathingal, J.G.4    Yen, S.H.5
  • 57
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher C, Brunner C, Lassmann H, Budka H, Jellinger K, et al. (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res 477: 90-99.
    • (1989) Brain Res , vol.477 , pp. 90-99
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3    Budka, H.4    Jellinger, K.5
  • 58
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz J, Chavez-Macias L, Garcia-Sierra F, Mena R, (2007) Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J Alzheimers Dis 12: 365-375.
    • (2007) J Alzheimers Dis , vol.12 , pp. 365-375
    • Luna-Munoz, J.1    Chavez-Macias, L.2    Garcia-Sierra, F.3    Mena, R.4
  • 59
    • 0040299037 scopus 로고    scopus 로고
    • AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease
    • Buee-Scherrer V, Condamines O, Mourton-Gilles C, Jakes R, Goedert M, et al. (1996) AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease. Brain Res Mol Brain Res 39: 79-88.
    • (1996) Brain Res Mol Brain Res , vol.39 , pp. 79-88
    • Buee-Scherrer, V.1    Condamines, O.2    Mourton-Gilles, C.3    Jakes, R.4    Goedert, M.5
  • 61
    • 82755177802 scopus 로고    scopus 로고
    • Stimulatory effect of alpha-synuclein on the tau-phosphorylation by GSK-3beta
    • Kawakami F, Suzuki M, Shimada N, Kagiya G, Ohta E, et al. (2011) Stimulatory effect of alpha-synuclein on the tau-phosphorylation by GSK-3beta. FEBS J 278: 4895-4904.
    • (2011) FEBS J , vol.278 , pp. 4895-4904
    • Kawakami, F.1    Suzuki, M.2    Shimada, N.3    Kagiya, G.4    Ohta, E.5
  • 62
    • 77955664249 scopus 로고    scopus 로고
    • Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia
    • Wills J, Jones J, Haggerty T, Duka V, Joyce JN, et al. (2010) Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia. Exp Neurol 225: 210-218.
    • (2010) Exp Neurol , vol.225 , pp. 210-218
    • Wills, J.1    Jones, J.2    Haggerty, T.3    Duka, V.4    Joyce, J.N.5
  • 63
    • 79952860574 scopus 로고    scopus 로고
    • Tauopathic changes in the striatum of A53T alpha-synuclein mutant mouse model of Parkinson's disease
    • Wills J, Credle J, Haggerty T, Lee JH, Oaks AW, et al. (2011) Tauopathic changes in the striatum of A53T alpha-synuclein mutant mouse model of Parkinson's disease. PLoS One 6: e17953.
    • (2011) PLoS One , vol.6
    • Wills, J.1    Credle, J.2    Haggerty, T.3    Lee, J.H.4    Oaks, A.W.5
  • 65
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels K, Van den Haute C, Van Dorpe J, Bruynseels K, Vandezande K, et al. (1999) Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am J Pathol 155: 2153-2165.
    • (1999) Am J Pathol , vol.155 , pp. 2153-2165
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3    Bruynseels, K.4    Vandezande, K.5
  • 66
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, et al. (2001) Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293: 711-714.
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5
  • 67
    • 0342803685 scopus 로고    scopus 로고
    • Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
    • Probst A, Gotz J, Wiederhold KH, Tolnay M, Mistl C, et al. (2000) Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein. Acta Neuropathol 99: 469-481.
    • (2000) Acta Neuropathol , vol.99 , pp. 469-481
    • Probst, A.1    Gotz, J.2    Wiederhold, K.H.3    Tolnay, M.4    Mistl, C.5
  • 68
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer C, Acker CM, Kress Y, Hof PR, Duff K, et al. (2005) Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 25: 5446-5454.
    • (2005) J Neurosci , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5
  • 69
    • 33646519920 scopus 로고    scopus 로고
    • Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • Spires TL, Orne JD, SantaCruz K, Pitstick R, Carlson GA, et al. (2006) Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy. Am J Pathol 168: 1598-1607.
    • (2006) Am J Pathol , vol.168 , pp. 1598-1607
    • Spires, T.L.1    Orne, J.D.2    SantaCruz, K.3    Pitstick, R.4    Carlson, G.A.5
  • 70
    • 20444372698 scopus 로고    scopus 로고
    • Alpha-synuclein targets the plasma membrane via the secretory pathway and induces toxicity in yeast
    • Dixon C, Mathias N, Zweig RM, Davis DA, Gross DS, (2005) Alpha-synuclein targets the plasma membrane via the secretory pathway and induces toxicity in yeast. Genetics 170: 47-59.
    • (2005) Genetics , vol.170 , pp. 47-59
    • Dixon, C.1    Mathias, N.2    Zweig, R.M.3    Davis, D.A.4    Gross, D.S.5
  • 71
    • 0042733228 scopus 로고    scopus 로고
    • Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor
    • Veal EA, Ross SJ, Malakasi P, Peacock E, Morgan BA, (2003) Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor. J Biol Chem 278: 30896-30904.
    • (2003) J Biol Chem , vol.278 , pp. 30896-30904
    • Veal, E.A.1    Ross, S.J.2    Malakasi, P.3    Peacock, E.4    Morgan, B.A.5
  • 72
    • 0347367068 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RAD5 influences the excision repair of DNA minor groove adducts
    • Kiakos K, Howard TT, Lee M, Hartley JA, McHugh PJ, (2002) Saccharomyces cerevisiae RAD5 influences the excision repair of DNA minor groove adducts. J Biol Chem 277: 44576-44581.
    • (2002) J Biol Chem , vol.277 , pp. 44576-44581
    • Kiakos, K.1    Howard, T.T.2    Lee, M.3    Hartley, J.A.4    McHugh, P.J.5
  • 73
    • 0029999229 scopus 로고    scopus 로고
    • The BUD4 protein of yeast, required for axial budding, is localized to the mother/BUD neck in a cell cycle-dependent manner
    • Sanders SL, Herskowitz I, (1996) The BUD4 protein of yeast, required for axial budding, is localized to the mother/BUD neck in a cell cycle-dependent manner. J Cell Biol 134: 413-427.
    • (1996) J Cell Biol , vol.134 , pp. 413-427
    • Sanders, S.L.1    Herskowitz, I.2
  • 74
    • 33646885472 scopus 로고    scopus 로고
    • alpha-Synuclein budding yeast model: toxicity enhanced by impaired proteasome and oxidative stress
    • Sharma N, Brandis KA, Herrera SK, Johnson BE, Vaidya T, et al. (2006) alpha-Synuclein budding yeast model: toxicity enhanced by impaired proteasome and oxidative stress. J Mol Neurosci 28: 161-178.
    • (2006) J Mol Neurosci , vol.28 , pp. 161-178
    • Sharma, N.1    Brandis, K.A.2    Herrera, S.K.3    Johnson, B.E.4    Vaidya, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.