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Volumn 1303, Issue , 2016, Pages 197-215

Yeast as a model for Alzheimer’s disease: Latest studies and advanced strategies

Author keywords

Alzheimer s disease; Amyloid beta; Model; Saccharomyces; Tau; Yeast

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; CALCIUM ION; GAMMA SECRETASE; HYBRID PROTEIN; PRION PROTEIN; TAU PROTEIN; PROTEIN AGGREGATE;

EID: 84938675333     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2627-5_11     Document Type: Article
Times cited : (22)

References (81)
  • 1
    • 10244239321 scopus 로고    scopus 로고
    • Life with 6000 genes
    • Goffeau A, Barrell BG, Bussey H et al (1996) Life with 6000 genes. Science 274(546): 563–567
    • (1996) Science , vol.274 , Issue.546 , pp. 563-567
    • Goffeau, A.1    Barrell, B.G.2    Bussey, H.3
  • 2
    • 33745482769 scopus 로고    scopus 로고
    • Yeastbased functional genomics and proteomics technologies: The first 15 years and beyond
    • Suter B, Auerbach D, Stagljar I (2006) Yeastbased functional genomics and proteomics technologies: the first 15 years and beyond. Biotechniques 40:625–644
    • (2006) Biotechniques , vol.40 , pp. 625-644
    • Suter, B.1    Auerbach, D.2    Stagljar, I.3
  • 3
    • 67650070937 scopus 로고    scopus 로고
    • Functional annotations for the Saccharomyces cerevisiae genome: The knowns and the known unknowns
    • Christie KR, Hong EL, Cherry JM (2009) Functional annotations for the Saccharomyces cerevisiae genome: the knowns and the known unknowns. Trends Microbiol 17:286–294
    • (2009) Trends Microbiol , vol.17 , pp. 286-294
    • Christie, K.R.1    Hong, E.L.2    Cherry, J.M.3
  • 5
    • 0030747938 scopus 로고    scopus 로고
    • Human genetic diseases: A cross-talk between man and yeast
    • Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195:1–10
    • (1997) Gene , vol.195 , pp. 1-10
    • Foury, F.1
  • 6
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman F (2002) Getting started with yeast. Methods Enzymol 350:3–41
    • (2002) Methods Enzymol , vol.350 , pp. 3-41
    • Sherman, F.1
  • 7
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. Cerevisiae genome by gene deletion and parallel analysis
    • Winzeler EA, Shoemaker DD, Astromoff A et al (1999) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285:901–906
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromoff, A.3
  • 8
    • 34147092780 scopus 로고    scopus 로고
    • Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae
    • Hu Y, Rolfs A, Bhullar B et al (2007) Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Genome Res 17: 536–543
    • (2007) Genome Res , vol.17 , pp. 536-543
    • Hu, Y.1    Rolfs, A.2    Bhullar, B.3
  • 9
    • 40149109321 scopus 로고    scopus 로고
    • A systematic library for comprehensive overexpression screens in Saccharomyces cerevisiae
    • Jones GM, Stalker J, Humphray S et al (2008) A systematic library for comprehensive overexpression screens in Saccharomyces cerevisiae. Nat Methods 5:239–241
    • (2008) Nat Methods , vol.5 , pp. 239-241
    • Jones, G.M.1    Stalker, J.2    Humphray, S.3
  • 10
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi JL, Iyer VR, Brown PO (1997) Exploring the metabolic and genetic control of gene expression on a genomic scale. Science 278:680–686
    • (1997) Science , vol.278 , pp. 680-686
    • Derisi, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 11
    • 52949145931 scopus 로고    scopus 로고
    • Yeast chemical genomics and drug discovery: An update
    • Hoon S, St Onge RP, Giaever G et al (2008) Yeast chemical genomics and drug discovery: an update. Trends Pharmacol Sci 29:499–504
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 499-504
    • Hoon, S.1    St Onge, R.P.2    Giaever, G.3
  • 12
    • 33746753342 scopus 로고    scopus 로고
    • Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast
    • Parsons AB, Lopez A, Givoni IE et al (2006) Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast. Cell 126:611–625
    • (2006) Cell , vol.126 , pp. 611-625
    • Parsons, A.B.1    Lopez, A.2    Givoni, I.E.3
  • 13
    • 18044372415 scopus 로고    scopus 로고
    • Yeast as a model for medical and medicinal research
    • Mager WH, Winderickx J (2005) Yeast as a model for medical and medicinal research. Trends Pharmacol Sci 26:265–273
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 265-273
    • Mager, W.H.1    Winderickx, J.2
  • 14
    • 77952741735 scopus 로고    scopus 로고
    • Modelling neurodegeneration in Saccharomyces cerevisiae: Why cook with baker’s yeast?
    • Khurana V, Lindquist S (2010) Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker’s yeast? Nat Rev Neurosci 11:436–449
    • (2010) Nat Rev Neurosci , vol.11 , pp. 436-449
    • Khurana, V.1    Lindquist, S.2
  • 15
    • 46549089111 scopus 로고    scopus 로고
    • Protein folding diseases and neurodegeneration: Lessons learned from yeast
    • Winderickx J, Delay C, De Vos A et al (2008) Protein folding diseases and neurodegeneration: lessons learned from yeast. Biochim Biophys Acta 1783:1381–1395
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1381-1395
    • Winderickx, J.1    Delay, C.2    De Vos, A.3
  • 16
    • 84880910987 scopus 로고    scopus 로고
    • The benefits of humanized yeast models to study Parkinson’s disease
    • Franssens V, Bynens T, Van den Brande J et al (2013) The benefits of humanized yeast models to study Parkinson’s disease. Oxid Med Cell Longev 2013:760629
    • (2013) Oxid Med Cell Longev , vol.2013
    • Franssens, V.1    Bynens, T.2    Van Den Brande, J.3
  • 17
    • 15944378475 scopus 로고    scopus 로고
    • Characterization of alpha-synuclein aggregation and synergistic toxicity with protein tau in yeast
    • Zabrocki P, Pellens K, Vanhelmont T 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
  • 18
    • 80053372157 scopus 로고    scopus 로고
    • Aggresome formation and segregation of inclusions influence toxicity of alpha-synuclein and synphilin-1 in yeast
    • Swinnen E, Buttner S, Outeiro TF et al (2011) Aggresome formation and segregation of inclusions influence toxicity of alpha-synuclein and synphilin-1 in yeast. Biochem Soc Trans 39:1476–1481
    • (2011) Biochem Soc Trans , vol.39 , pp. 1476-1481
    • Swinnen, E.1    Buttner, S.2    Outeiro, T.F.3
  • 19
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S, Lindquist S (2000) Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci U S A 97:1589–1594
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 20
    • 0034608868 scopus 로고    scopus 로고
    • Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
    • Muchowski PJ, Schaffar G, Sittler A et al (2000) Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc Natl Acad Sci U S A 97:7841–7846
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7841-7846
    • Muchowski, P.J.1    Schaffar, G.2    Sittler, A.3
  • 21
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prionlike protein Rnq 1
    • Meriin AB, Zhang X, He X et al (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prionlike protein Rnq 1. J Cell Biol 157:997–1004
    • (2002) J Cell Biol , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3
  • 22
    • 80053349243 scopus 로고    scopus 로고
    • Using yeast models to probe the molecular basis of amyotrophic lateral sclerosis
    • Bastow EL, Gourlay CW, Tuite MF (2011) Using yeast models to probe the molecular basis of amyotrophic lateral sclerosis. Biochem Soc Trans 39:1482–1487
    • (2011) Biochem Soc Trans , vol.39 , pp. 1482-1487
    • Bastow, E.L.1    Gourlay, C.W.2    Tuite, M.F.3
  • 23
    • 60449092020 scopus 로고    scopus 로고
    • ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy
    • Fu L, Sztul E (2009) ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy. Eur J Cell Biol 88:215–226
    • (2009) Eur J Cell Biol , vol.88 , pp. 215-226
    • Fu, L.1    Sztul, E.2
  • 24
    • 10944223484 scopus 로고    scopus 로고
    • Tau protein as a differential biomarker of tauopathies
    • Sergeant N, Delacourte A, Buee L (2005) Tau protein as a differential biomarker of tauopathies. Biochim Biophys Acta 1739:179–197
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 179-197
    • Sergeant, N.1    Delacourte, A.2    Buee, L.3
  • 25
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases—new features and familiar faces
    • Esler WP, Wolfe MS (2001) A portrait of Alzheimer secretases—new features and familiar faces. Science 293:1449–1454
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 26
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper B, Annaert W (2000) Proteolytic processing and cell biological functions of the amyloid precursor protein. J Cell Sci 113: 1857–1870
    • (2000) J Cell Sci , vol.113 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 27
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of betaamyloid precursor protein is inhibited by zinc in Alzheimer’s disease
    • Duce JA, Tsatsanis A, Cater MA et al (2010) Iron-export ferroxidase activity of betaamyloid precursor protein is inhibited by zinc in Alzheimer’s disease. Cell 142:857–867
    • (2010) Cell , vol.142 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3
  • 28
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: Proteasome of the membrane?
    • Kopan R, Ilagan MX (2004) Gamma-secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 5:499–504
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 29
    • 57649174625 scopus 로고    scopus 로고
    • Intramembrane proteolysis by gammasecretase
    • Steiner H, Fluhrer R, Haass C (2008) Intramembrane proteolysis by gammasecretase. J Biol Chem 283:29627–29631
    • (2008) J Biol Chem , vol.283 , pp. 29627-29631
    • Steiner, H.1    Fluhrer, R.2    Haass, C.3
  • 30
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • Turner PR, O’Connor K, Tate WP et al (2003) Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog Neurobiol 70:1–32
    • (2003) Prog Neurobiol , vol.70 , pp. 1-32
    • Turner, P.R.1    O’Connor, K.2    Tate, W.P.3
  • 31
    • 34447316702 scopus 로고    scopus 로고
    • Genetics of Alzheimer’s disease: A centennial review
    • Ertekin-Taner N (2007) Genetics of Alzheimer’s disease: a centennial review. Neurol Clin 25:611–667
    • (2007) Neurol Clin , vol.25 , pp. 611-667
    • Ertekin-Taner, N.1
  • 32
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer’s disease
    • LaFerla FM, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer’s disease. Nat Rev Neurosci 8:499–509
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 33
    • 33746930858 scopus 로고    scopus 로고
    • Trafficking of Alzheimer’s disease-related membrane proteins and its participation in disease pathogenesis
    • Suzuki T, Araki Y, Yamamoto T et al (2006) Trafficking of Alzheimer’s disease-related membrane proteins and its participation in disease pathogenesis. J Biochem 139:949–955
    • (2006) J Biochem , vol.139 , pp. 949-955
    • Suzuki, T.1    Araki, Y.2    Yamamoto, T.3
  • 34
    • 33644849690 scopus 로고    scopus 로고
    • Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments
    • Vetrivel KS, Thinakaran G (2006) Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments. Neurology 66(2 Suppl 1):S69–S73
    • (2006) Neurology , vol.66 , Issue.2-1 , pp. S69-S73
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 35
    • 33646461282 scopus 로고    scopus 로고
    • Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH, Gouras GK (2006) Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 26:4277–4288
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 36
    • 34250211094 scopus 로고    scopus 로고
    • Mitochondrial Abeta: A potential cause of metabolic dysfunction in Alzheimer’s disease
    • Chen X, Yan SD (2006) Mitochondrial Abeta: a potential cause of metabolic dysfunction in Alzheimer’s disease. IUBMB Life 58: 686–694
    • (2006) IUBMB Life , vol.58 , pp. 686-694
    • Chen, X.1    Yan, S.D.2
  • 37
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor proteinmediated free radicals and oxidative damage: Implications for the development and progression of Alzheimer’s disease
    • Reddy PH (2006) Amyloid precursor proteinmediated free radicals and oxidative damage: implications for the development and progression of Alzheimer’s disease. J Neurochem 96:1–13
    • (2006) J Neurochem , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 38
    • 33748934403 scopus 로고    scopus 로고
    • Alzheimer’s disease and endocytic dysfunction: Clues from the Down syndrome-related proteins, DSCR1 and ITSN 1
    • Keating DJ, Chen C, Pritchard MA (2006) Alzheimer’s disease and endocytic dysfunction: clues from the Down syndrome-related proteins, DSCR1 and ITSN 1. Ageing Res Rev 5:388–401
    • (2006) Ageing Res Rev , vol.5 , pp. 388-401
    • Keating, D.J.1    Chen, C.2    Pritchard, M.A.3
  • 39
    • 11244317067 scopus 로고    scopus 로고
    • Alzheimer’s amyloid peptides mediate hypoxic up-regulation of L-type Ca 2+ channels
    • Scragg JL, Fearon IM, Boyle JP et al (2005) Alzheimer’s amyloid peptides mediate hypoxic up-regulation of L-type Ca 2+ channels. FASEB J 19:150–152
    • (2005) FASEB J , vol.19 , pp. 150-152
    • Scragg, J.L.1    Fearon, I.M.2    Boyle, J.P.3
  • 40
    • 33644516276 scopus 로고    scopus 로고
    • Molecular dissection of the interaction between amyloid precursor protein and its neuronal trafficking receptor SorLA/LR 11
    • Andersen OM, Schmidt V, Spoelgen R et al (2006) Molecular dissection of the interaction between amyloid precursor protein and its neuronal trafficking receptor SorLA/LR 11. Biochemistry 45:2618–2628
    • (2006) Biochemistry , vol.45 , pp. 2618-2628
    • Andersen, O.M.1    Schmidt, V.2    Spoelgen, R.3
  • 41
    • 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 (1994) Proteolytic processing and secretion of human beta-amyloid precursor protein in yeast. Evidence for a yeast secretase activity. J Biol Chem 269:27799–27802
    • (1994) J Biol Chem , vol.269 , pp. 27799-27802
    • Zhang, H.1    Komano, H.2    Fuller, R.S.3
  • 42
    • 0030700930 scopus 로고    scopus 로고
    • Characterization of beta-amyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases
    • Zhang W, Espinoza D, Hines V et al (1997) Characterization of beta-amyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases. Biochim Biophys Acta 1359: 110–122
    • (1997) Biochim Biophys Acta , vol.1359 , pp. 110-122
    • Zhang, W.1    Espinoza, D.2    Hines, V.3
  • 43
    • 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 (2003) Human beta-secretase activity in yeast detected by a novel cellular growth selection system. Biochim Biophys Acta 1620:167–178
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 167-178
    • Luthi, U.1    Schaerer-Brodbeck, C.2    Tanner, S.3
  • 44
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of gamma-secretase activity
    • Edbauer D, Winkler E, Regula JT et al (2003) Reconstitution of gamma-secretase activity. Nat Cell Biol 5:486–488
    • (2003) Nat Cell Biol , vol.5 , pp. 486-488
    • Edbauer, D.1    Winkler, E.2    Regula, J.T.3
  • 45
    • 34748873815 scopus 로고    scopus 로고
    • Proteomic analysis of the amyloid precursor protein fragment C99: Expression in yeast
    • Sparvero LJ, Patz S, Brodsky JL et al (2007) Proteomic analysis of the amyloid precursor protein fragment C99: expression in yeast. Anal Biochem 370:162–170
    • (2007) Anal Biochem , vol.370 , pp. 162-170
    • Sparvero, L.J.1    Patz, S.2    Brodsky, J.L.3
  • 46
    • 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, Antony H et al (2007) Alzheimer’s Abeta fused to green fluorescent protein induces growth stress and a heat shock response. FEMS Yeast Res 7:1230–1236
    • (2007) FEMS Yeast Res , vol.7 , pp. 1230-1236
    • Caine, J.1    Sankovich, S.2    Antony, H.3
  • 47
    • 82755197062 scopus 로고    scopus 로고
    • Functional links between Abeta toxicity, endocytic trafficking, and Alzheimer’s disease risk factors in yeast
    • Treusch S, Hamamichi S, Goodman JL et al (2011) Functional links between Abeta toxicity, endocytic trafficking, and Alzheimer’s disease risk factors in yeast. Science 334:1241–1245
    • (2011) Science , vol.334 , pp. 1241-1245
    • Treusch, S.1    Hamamichi, S.2    Goodman, J.L.3
  • 48
    • 70349558522 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer’s disease
    • Harold D, Abraham R, Hollingworth P et al (2009) Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer’s disease. Nat Genet 41: 1088–1093
    • (2009) Nat Genet , vol.41 , pp. 1088-1093
    • Harold, D.1    Abraham, R.2    Hollingworth, P.3
  • 49
    • 78549264026 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer’s disease
    • Lambert JC, Heath S, Even G et al (2009) Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer’s disease. Nat Genet 41:1094–1099
    • (2009) Nat Genet , vol.41 , pp. 1094-1099
    • Lambert, J.C.1    Heath, S.2    Even, G.3
  • 50
    • 84872085620 scopus 로고    scopus 로고
    • A yeast model for amyloid-beta aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity
    • D’Angelo F, Vignaud H, Di Martino J et al (2013) A yeast model for amyloid-beta aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity. Dis Model Mech 6:206–216
    • (2013) Dis Model Mech , vol.6 , pp. 206-216
    • D’Angelo, F.1    Vignaud, H.2    Di Martino, J.3
  • 51
    • 33750010673 scopus 로고    scopus 로고
    • Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system
    • Bagriantsev S, Liebman S (2006) Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system. BMC Biol 4:32
    • (2006) BMC Biol , vol.4 , pp. 32
    • Bagriantsev, S.1    Liebman, S.2
  • 52
    • 81455128231 scopus 로고    scopus 로고
    • Development and validation of a yeast highthroughput screen for inhibitors of Abeta(4) (2) oligomerization
    • Park SK, Pegan SD, Mesecar AD et al (2011) Development and validation of a yeast highthroughput screen for inhibitors of Abeta(4) (2) oligomerization. Dis Model Mech 4: 822–831
    • (2011) Dis Model Mech , vol.4 , pp. 822-831
    • Park, S.K.1    Pegan, S.D.2    Mesecar, A.D.3
  • 53
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee L, Bussiere T, Buee-Scherrer V et al (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 33:95–130
    • (2000) Brain Res Brain Res Rev , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3
  • 54
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • Maas T, Eidenmuller J, Brandt R (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem 275:15733–15740
    • (2000) J Biol Chem , vol.275 , pp. 15733-15740
    • Maas, T.1    Eidenmuller, J.2    Brandt, R.3
  • 55
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau’s amino-terminal projection domain
    • Brandt R, Leger J, Lee G (1995) Interaction of tau with the neural plasma membrane mediated by tau’s amino-terminal projection domain. J Cell Biol 131:1327–1340
    • (1995) J Cell Biol , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 56
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga TA, Elson-Schwab I, Khurana V et al (2007) Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 9: 139–148
    • (2007) Nat Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3
  • 57
    • 79251588043 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau by the SRC family kinases lck and fyn
    • Scales TM, Derkinderen P, Leung KY et al (2011) Tyrosine phosphorylation of tau by the SRC family kinases lck and fyn. Mol Neurodegener 6:12
    • (2011) Mol Neurodegener , vol.6 , pp. 12
    • Scales, T.M.1    Derkinderen, P.2    Leung, K.Y.3
  • 58
    • 10944228450 scopus 로고    scopus 로고
    • Tau and src family tyrosine kinases
    • Lee G (2005) Tau and src family tyrosine kinases. Biochim Biophys Acta 1739:323–330
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 323-330
    • Lee, G.1
  • 59
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau—a toxic pas de deux in Alzheimer’s disease
    • Ittner LM, Gotz J (2011) Amyloid-beta and tau—a toxic pas de deux in Alzheimer’s disease. Nat Rev Neurosci 12:65–72
    • (2011) Nat Rev Neurosci , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 60
    • 43449128899 scopus 로고    scopus 로고
    • Biochemistry of Tau in Alzheimer’s disease and related neurological disorders
    • Sergeant N, Bretteville A, Hamdane M et al (2008) Biochemistry of Tau in Alzheimer’s disease and related neurological disorders. Expert Rev Proteomics 5:207–224
    • (2008) Expert Rev Proteomics , vol.5 , pp. 207-224
    • Sergeant, N.1    Bretteville, A.2    Hamdane, M.3
  • 64
    • 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 (2005) Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 44:11466–11475
    • (2005) Biochemistry , vol.44 , pp. 11466-11475
    • Vandebroek, T.1    Vanhelmont, T.2    Terwel, D.3
  • 65
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50’s selectivity for Alzheimer’s disease pathology
    • Carmel G, Mager EM, Binder LI et al (1996) The structural basis of monoclonal antibody Alz50’s selectivity for Alzheimer’s disease pathology. J Biol Chem 271:32789–32795
    • (1996) J Biol Chem , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3
  • 66
    • 0034594482 scopus 로고    scopus 로고
    • Formation of diffuse and fibrillar tangles in aging and early Alzheimer’s disease
    • Uboga NV, Price JL (2000) Formation of diffuse and fibrillar tangles in aging and early Alzheimer’s disease. Neurobiol Aging 21:1–10
    • (2000) Neurobiol Aging , vol.21 , pp. 1-10
    • Uboga, N.V.1    Price, J.L.2
  • 67
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer’s disease
    • Weaver CL, Espinoza M, Kress Y et al (2000) Conformational change as one of the earliest alterations of tau in Alzheimer’s disease. Neurobiol Aging 21:719–727
    • (2000) Neurobiol Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3
  • 68
    • 0344011447 scopus 로고    scopus 로고
    • Decreased cyclin-dependent kinase 5 (Cdk5) activity is accompanied by redistribution of cdk5 and cytoskeletal proteins and increased cytoskeletal protein phosphorylation in p35 null mice
    • Hallows JL, Chen K, DePinho RA et al (2003) Decreased cyclin-dependent kinase 5 (cdk5) activity is accompanied by redistribution of cdk5 and cytoskeletal proteins and increased cytoskeletal protein phosphorylation in p35 null mice. J Neurosci 23:10633–10644
    • (2003) J Neurosci , vol.23 , pp. 10633-10644
    • Hallows, J.L.1    Chen, K.2    Depinho, R.A.3
  • 69
    • 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 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
  • 70
    • 0033198043 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase phosphorylations on tau in Alzheimer’s disease
    • Jicha GA, Weaver C, Lane E et al (1999) cAMP-dependent protein kinase phosphorylations on tau in Alzheimer’s disease. J Neurosci 19:7486–7494
    • (1999) J Neurosci , vol.19 , pp. 7486-7494
    • Jicha, G.A.1    Weaver, C.2    Lane, E.3
  • 71
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filamentlike conformation
    • Zheng-Fischhofer Q, Biernat J, Mandelkow EM et al (1998) Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filamentlike conformation. Eur J Biochem 252: 542–552
    • (1998) Eur J Biochem , vol.252 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3
  • 72
    • 40449087334 scopus 로고    scopus 로고
    • Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3 beta mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing
    • Wen Y, Planel E, Herman M et al (2008) Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3 beta mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing. J Neurosci 28:2624–2632
    • (2008) J Neurosci , vol.28 , pp. 2624-2632
    • Wen, Y.1    Planel, E.2    Herman, M.3
  • 73
    • 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 cdk 5
    • Vandebroek T, Terwel D, Vanhelmont T 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 cdk 5. J Biol Chem 281:25388–25397
    • (2006) J Biol Chem , vol.281 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3
  • 74
    • 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 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
  • 75
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • Gamblin TC, Berry RW, Binder LI (2003) Tau polymerization: role of the amino terminus. Biochemistry 42:2252–2257
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 76
    • 77957871737 scopus 로고    scopus 로고
    • Alzheimer’s proteins, oxidative stress, and mitochondrial dysfunction interplay in a neuronal model of Alzheimer’s disease
    • Bobba A, Petragallo VA, Marra E et al (2010) Alzheimer’s proteins, oxidative stress, and mitochondrial dysfunction interplay in a neuronal model of Alzheimer’s disease. Int J Alzheimers Dis 621870, 11 pg
    • (2010) Int J Alzheimers Dis , pp. 11
    • Bobba, A.1    Petragallo, V.A.2    Marra, E.3
  • 77
    • 75949083202 scopus 로고    scopus 로고
    • Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates
    • Martinez A, Portero-Otin M, Pamplona R et al (2010) Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol 20:281–297
    • (2010) Brain Pathol , vol.20 , pp. 281-297
    • Martinez, A.1    Portero-Otin, M.2    Pamplona, R.3
  • 78
    • 38849150935 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress causes hyperphosphorylation of tau
    • Melov S, Adlard PA, Morten K et al (2007) Mitochondrial oxidative stress causes hyperphosphorylation of tau. PLoS One 2:e536
    • (2007) Plos One , vol.2
    • Melov, S.1    Adlard, P.A.2    Morten, K.3
  • 79
    • 42049116923 scopus 로고    scopus 로고
    • Alzheimer disease and the role of free radicals in the pathogenesis of the disease
    • Moreira PI, Santos MS, Oliveira CR et al (2008) Alzheimer disease and the role of free radicals in the pathogenesis of the disease. CNS Neurol Disord Drug Targets 7:3–10
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , pp. 3-10
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 80
    • 0039604509 scopus 로고
    • A yeast mutant lacking mitochondrial manganese- superoxide dismutase is hypersensitive to oxygen
    • Van Loon AP, Pesold-Hurt B, Schatz G (1986) A yeast mutant lacking mitochondrial manganese- superoxide dismutase is hypersensitive to oxygen. Proc Natl Acad Sci U S A 83:3820–3824
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3820-3824
    • Van Loon, A.P.1    Pesold-Hurt, B.2    Schatz, G.3
  • 81
    • 0026784158 scopus 로고
    • A single-stranded DNA binding protein required for mitochondrial DNA replication in S. Cerevisiae is homologous to E. Coli SSB
    • Van Dyck E, Foury F, Stillman B et al (1992) A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB. EMBO J 11:3421–3430
    • (1992) EMBO J , vol.11 , pp. 3421-3430
    • Van Dyck, E.1    Foury, F.2    Stillman, B.3


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