메뉴 건너뛰기




Volumn 66, Issue 8, 2009, Pages 635-649

Cytoskeletal pathologies of Alzheimer disease

Author keywords

Actin; Alzheimer disease; Amyloid beta; Cofilin; Microtubule; Tau

Indexed keywords

ACTIN BINDING PROTEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; COFILIN; G ACTIN; TAU PROTEIN;

EID: 67749133983     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20388     Document Type: Review
Times cited : (131)

References (175)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew BJ, Minamide LS, Bamburg JR. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270:17582-17587.
    • (1995) J Biol Chem , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 3
    • 0019973602 scopus 로고
    • Monoclonal antibodies show that neurofibrillary tangles and neurofilaments share antigenic determinants
    • DOI 10.1038/298084a0
    • Anderton BH, Breinburg D, Downes MJ, Green PJ, Tomlinson BE, Ulrich J, Wood JN, Kahn J. 1982. Monoclonal antibodies show that neurofibrillary tangles and neurofilaments share antigenic determinants. Nature 298:84-86. (Pubitemid 12087486)
    • (1982) Nature , vol.298 , Issue.5869 , pp. 84-86
    • Anderton, B.H.1    Breinburg, D.2    Downes, M.J.3
  • 4
    • 10944272640 scopus 로고    scopus 로고
    • Tau gene alternative splicing: Expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases
    • DOI 10.1016/j.bbadis.2004.08.010, PII S0925443904001541
    • Andreadis A. 2005. Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases. Biochim Biophys Acta 1739:91-103. (Pubitemid 40018532)
    • (2005) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1739 , Issue.2 , pp. 91-103
    • Andreadis, A.1
  • 5
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of Actin Filament Turnover by Severing and Nucleation at Different Concentrations of ADF/Cofilin
    • DOI 10.1016/j.molcel.2006.08.006, PII S109727650600565X
    • Andrianantoandro E, Pollard TD. 2006. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell 24:13-23. (Pubitemid 44466682)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 6
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM- Kinase
    • DOI 10.1038/31729
    • Arber S, Barbayannis FA, Hanser H, Schneider C, Stanyon CA, Bernard O, Caroni P. 1998. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393:805-809. (Pubitemid 28299494)
    • (1998) Nature , vol.393 , Issue.6687 , pp. 805-809
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3    Schnelder, C.4    Stanyon, C.A.5    Bernards, O.6    Caroni, P.7
  • 10
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg JR, Wiggan OP. 2002. ADF/cofilin and actin dynamics in disease. Trends Cell Biol 12:598-605.
    • (2002) Trends Cell Biol , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 11
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • DOI 10.1016/0014-5793(93)80849-P
    • Baumann K, Mandelkow EM, Biernat J, Piwnica-Worms H, Mandelkow E. 1993. Abnormal Alzheimer's-like phosphorylation of tau protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett 335:171-175. (Pubitemid 24036992)
    • (1993) FEBS Letters , vol.336 , Issue.3 , pp. 417-424
    • Baumann, K.1
  • 12
    • 33751082967 scopus 로고    scopus 로고
    • Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons
    • DOI 10.1152/ajpcell.00066.2006
    • Bernstein BW, Chen H, Boyle JA, Bamburg JR. 2006. Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons. Am J Physiol Cell Physiol 291:C828-C839. (Pubitemid 44771802)
    • (2006) American Journal of Physiology - Cell Physiology , vol.291 , Issue.5
    • Bernstein, B.W.1    Chen, H.2    Boyle, J.A.3    Bamburg, J.R.4
  • 13
    • 84864813489 scopus 로고    scopus 로고
    • Actin and diseases of the nervous system
    • Gallo G, Lanier LL, editors. Springer. In press
    • Bernstein BW, Maloney MT, Bamburg JR. Actin and diseases of the nervous system. In: Gallo G, Lanier LL, editors. Neurobiology of Actin. Springer. In press.
    • Neurobiology of Actin
    • Bernstein, B.W.1    Maloney, M.T.2    Bamburg, J.R.3
  • 14
    • 0018938686 scopus 로고
    • Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism
    • Bershadsky AD, Gelfand VI, Svitkina TM, Tint IS. 1980. Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism. Exp Cell Res 127:421-429.
    • (1980) Exp Cell Res , vol.127 , pp. 421-429
    • Bershadsky, A.D.1    Gelfand, V.I.2    Svitkina, T.M.3    Tint, I.S.4
  • 15
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11:153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 16
    • 0022365608 scopus 로고
    • The distribution of tau in the nervous system
    • Binder LI, Frankfurter A, Rebhun LI. 1985. The distribution of tau in the nervous system. J Cell Biol 101:1371-1378.
    • (1985) J Cell Biol , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 17
    • 0032559708 scopus 로고    scopus 로고
    • Cruising along microtubule highways: How membranes move through the secretory pathway
    • Bloom GS, Goldstein LSB. 1998. Cruising along microtubule highways: how membranes move through the secretory pathway. J Cell Biol 140:1277-1280.
    • (1998) J Cell Biol , vol.140 , pp. 1277-1280
    • Bloom, G.S.1    Goldstein, L.S.B.2
  • 18
    • 0028982504 scopus 로고
    • Distribution of Big tau in the central nervous system of the adult and developing rat
    • Boyne LJ, Tessler A, Murray M, Fischer I. 1995. Distribution of Big tau in the central nervous system of the adult and developing rat. J Comp Neurol 358:279-293.
    • (1995) J Comp Neurol , vol.358 , pp. 279-293
    • Boyne, L.J.1    Tessler, A.2    Murray, M.3    Fischer, I.4
  • 19
    • 34548225942 scopus 로고    scopus 로고
    • Control of synaptic consolidation in the dentate gyrus: Mechanisms, functions, and therapeutic implications
    • Bramham CR. 2007. Control of synaptic consolidation in the dentate gyrus: mechanisms, functions, and therapeutic implications. Prog Brain Res 163:453-471.
    • (2007) Prog Brain Res , vol.163 , pp. 453-471
    • Bramham, C.R.1
  • 20
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • DOI 10.1016/S0165-0173(00)00019-9, PII S0165017300000199
    • Buée L, Bussiere T, Buée-Scherrer V, Delacourte A, Hof PR. 2000. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Rev 33:95-130. (Pubitemid 30680029)
    • (2000) Brain Research Reviews , vol.33 , Issue.1 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 21
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J, Lorenzo A, Yankner BA. 1992. Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol Aging 13:609-612.
    • (1992) Neurobiol Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 22
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • DOI 10.1074/jbc.R900037199
    • Calderwood DA, Shattil SJ, Ginsberg MH. 2000. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem 275:22607-22610. (Pubitemid 30646138)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 23
    • 58149379613 scopus 로고    scopus 로고
    • SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin
    • Carlisle HJ, Manzerra P, Marcora E, Kennedy MB. 2008. SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin. J Neurosci 28:13673-13683.
    • (2008) J Neurosci , vol.28 , pp. 13673-13683
    • Carlisle, H.J.1    Manzerra, P.2    Marcora, E.3    Kennedy, M.B.4
  • 25
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased β-amyloidogenesis
    • Cataldo AM, Barnett JL, Pieroni C, Nixon RA. 1997. Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J Neurosci 17:6142-6151. (Pubitemid 27329890)
    • (1997) Journal of Neuroscience , vol.17 , Issue.16 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 26
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid β deposition in sporadic alzheimer's disease and down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo AM, Peterhoff CM, Troncoso JC, Gomez-Isla T, Hyman BT, Nixon RA. 2000. Endocytic pathway abnormalities precede amyloid-β deposition in sporadic Alzheimer's disease and Down syndrome. Differential effects of ApoE genotype and presenilin mutations. Am J Pathol 157:277-286. (Pubitemid 30641743)
    • (2000) American Journal of Pathology , vol.157 , Issue.1 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 29
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • Chan C, Beltzner CC, Pollard TD. 2009. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr Biol 19:537-545.
    • (2009) Curr Biol , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 32
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • Chen H, Bernstein BW, Sneider JM, Boyle JA, Minamide LS, Bamburg JR. 2004. In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 43:7127-7142.
    • (2004) Biochemistry , vol.43 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5    Bamburg, J.R.6
  • 33
    • 12844269955 scopus 로고    scopus 로고
    • Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development
    • DOI 10.1128/MCB.25.3.979-987.2005
    • Chen GC, Turano B, Ruest PJ, Hagel M, Settleman J, Thomas SM. 2005. Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development. Mol Cell Biol 25:979-987. (Pubitemid 40165806)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.3 , pp. 979-987
    • Chen, G.-C.1    Turano, B.2    Ruest, P.J.3    Hagel, M.4    Settleman, J.5    Thomas, S.M.6
  • 34
    • 30744439325 scopus 로고    scopus 로고
    • Cdc42 participates in the regulation of ADF/cofilin and retinal growth cone filopodia by brain derived neurotrophic factor
    • DOI 10.1002/neu.20204
    • Chen TJ, Gehler S, Shaw AE, Bamburg JR, Letourneau PC. 2006. Cdc42 participates in regulation of ADF/cofilin and retinal growth cone filopodia by brain derived neurotrophic factor. J Neurobiol 66:103-114. (Pubitemid 43100725)
    • (2006) Journal of Neurobiology , vol.66 , Issue.2 , pp. 103-114
    • Chen, T.-J.1    Gehler, S.2    Shaw, A.E.3    Bamburg, J.R.4    Letourneau, P.C.5
  • 35
    • 40549129366 scopus 로고    scopus 로고
    • Disrupted intracellular calcium regulates BACE1 gene expression via nuclear factor of activated T cells 1 (NFAT 1) signaling
    • DOI 10.1111/j.1474-9726.2007.00360.x
    • Cho HJ, Jim SM, Youn HD, Huh K, Mook-Jung I. 2008. Disrupted intracellular calcium regulates BACE1 gene expression via nuclear factor of activated T cells 1 (NFAT1) signaling. Aging Cell 7:137-147. (Pubitemid 351359647)
    • (2008) Aging Cell , vol.7 , Issue.2 , pp. 137-147
    • Cho, H.-J.1    Jin, S.M.2    Youn, H.D.3    Huh, K.4    Mook-Jung, I.5
  • 38
    • 38349002996 scopus 로고    scopus 로고
    • A cell culture model for investigation of Hirano bodies
    • Davis RC, Furukawa R, Fechheimer M. 2008. A cell culture model for investigation of Hirano bodies. Acta Neuropathol 115:205-217.
    • (2008) Acta Neuropathol , vol.115 , pp. 205-217
    • Davis, R.C.1    Furukawa, R.2    Fechheimer, M.3
  • 40
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • DOI 10.1074/jbc.M607483200
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL. 2007. Abeta oligomers induce neuronal oxidative stress through an N-methy-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:1590-1601. (Pubitemid 47100810)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 42
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • DOI 10.1523/JNEUROSCI.1189-06.2006
    • Deshpande A, Mina E, Glabe C, Busciglio J. 2006. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J Neurosci 26:6011-6018. (Pubitemid 44318367)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 45
    • 44049089120 scopus 로고    scopus 로고
    • Vascular risk factors, cognitve decline, and dementia
    • Duron E, Hanon O. 2008. Vascular risk factors, cognitive decline and dementia. Vasc Health Risk Manag 4:363-381. (Pubitemid 351711965)
    • (2008) Vascular Health and Risk Management , vol.4 , Issue.2 , pp. 363-381
    • Duron, E.1    Hanon, O.2
  • 46
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards DC, Sanders LC, Bokoch GM, Gill GN. 1999. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1:253-259.
    • (1999) Nat Cell Biol , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 47
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. 2003. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160:113-123. (Pubitemid 36091721)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 48
    • 67349096401 scopus 로고    scopus 로고
    • Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot
    • Eiseler T, Doppler H, Yan IK, Kitatani K, Mizuno K, Storz P. 2009. Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot. Nat Cell Biol 11:545-556.
    • (2009) Nat Cell Biol , vol.11 , pp. 545-556
    • Eiseler, T.1    Doppler, H.2    Yan, I.K.3    Kitatani, K.4    Mizuno, K.5    Storz, P.6
  • 49
    • 42749087763 scopus 로고    scopus 로고
    • The mitochondrial impairment, oxidative stress and neurodegeneration connection: Reality of just an attractive hypothesis
    • Fukui H, Moraes CT. 2008. The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality of just an attractive hypothesis. Trends Neurosci 31:251-256.
    • (2008) Trends Neurosci , vol.31 , pp. 251-256
    • Fukui, H.1    Moraes, C.T.2
  • 51
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • DOI 10.1083/jcb.153.1.75
    • Galkin VE, Orlova A, Lukoyanova N, Wriggers W, Engelman EH. 2001. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol 153:75-86. (Pubitemid 34280195)
    • (2001) Journal of Cell Biology , vol.153 , Issue.1 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggersd, W.4    Egelman, E.H.5
  • 54
    • 0034929144 scopus 로고    scopus 로고
    • Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease
    • DOI 10.1016/S0891-0618(01)00096-5, PII S0891061801000965
    • García-Sierra F, Wischik CM, Harrington CR, Luna-Muñoz J, Mena R. 2001. Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology of Alzheimer's disease. J Chem Neuroanat 22:65-77. (Pubitemid 32695510)
    • (2001) Journal of Chemical Neuroanatomy , vol.22 , Issue.1-2 , pp. 65-77
    • Garcia-Sierra, F.1    Wischik, C.M.2    Harrington, C.R.3    Luna-Munoz, J.4    Mena, R.5
  • 57
    • 0017642031 scopus 로고
    • Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer's disease
    • Gibson PH, Tomlinson BE. 1977. Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer's disease. J Neurol Sci 33:199-206.
    • (1977) J Neurol Sci , vol.33 , pp. 199-206
    • Gibson, P.H.1    Tomlinson, B.E.2
  • 58
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. 1984a. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890. (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 59
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. 1984b. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 122:1131-1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 61
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M, Spillantini MG, Potier MC, Ulrich J, Crowther RA. 1989a. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J 8:393-399. (Pubitemid 19274956)
    • (1989) EMBO Journal , vol.8 , Issue.2 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 62
    • 0024745894 scopus 로고
    • Multiple forms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. 1989b. Multiple forms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3:519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 63
    • 0026784416 scopus 로고
    • p42 map kinase phosphorylation sites in MT-associated protein tau are dephosphorylated by protein phosphatase 2A: Implications for Alzheimer's disease
    • Goedert M, Cohen ES, Jakes R, Cohen P. 1992. p42 map kinase phosphorylation sites in MT-associated protein tau are dephosphorylated by protein phosphatase 2A: implications for Alzheimer's disease. FEBS Lett 312:95-99.
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 64
    • 0028885494 scopus 로고
    • Protein phosphatase 2A is the major enzyme in brain that dephosphorylates τ protein phosphorylated by proline-directed protein kinases or cyclic-AMP-dependent protein kinase
    • Goedert M, Jakes R, Qi Z, Wang JH, Cohen P. 1995. Protein phosphatase 2A is the major enzyme in brain that dephosphorylates τ protein phosphorylated by proline-directed protein kinases or cyclic-AMP-dependent protein kinase. J Neurochem 65:2804-2807.
    • (1995) J Neurochem , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 65
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • DOI 10.1038/383550a0
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA. 1996. Assembly of microtubule-associated protein tau into Alzheimer's-like filaments induced by sulphated glycosaminoglycans. Nature 383:550-553. (Pubitemid 26346185)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 66
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • DOI 10.1038/ncb1201
    • Gohla A, Birkenfeld J, Bokoch GM. 2005. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7:21-29. (Pubitemid 40123379)
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 67
    • 33745038221 scopus 로고    scopus 로고
    • Inhibition of APP trafficking by tau protein does not increase the generation of amyloid-β peptides
    • DOI 10.1111/j.1600-0854.2006.00434.x
    • Goldsbury C, Mocanu MM, Thies E, Kaether C, Haass C, Keller P, Biernat J, Mandelkow E, Mandelkow EM. 2006. Inhibition of APP trafficking by tau protein does not increase the generation of amyloid-beta peptides. Traffic 7:873-888. (Pubitemid 43871776)
    • (2006) Traffic , vol.7 , Issue.7 , pp. 873-888
    • Goldsbury, C.1    Mocanu, M.-M.2    Thies, E.3    Kaether, C.4    Haass, C.5    Keller, P.6    Biernat, J.7    Mandelkow, E.8    Mandelkow, E.-M.9
  • 68
    • 52649131924 scopus 로고    scopus 로고
    • Oxidative stress increases levels of endogenous amyloid-beta peptides secreted from primary chick brain neurons
    • Goldsbury C, Whiteman IT, Jeong EV, Lim YA. 2008. Oxidative stress increases levels of endogenous amyloid-beta peptides secreted from primary chick brain neurons. Aging Cell 7:771-775.
    • (2008) Aging Cell , vol.7 , pp. 771-775
    • Goldsbury, C.1    Whiteman, I.T.2    Jeong, E.V.3    Lim, Y.A.4
  • 70
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils
    • DOI 10.1126/science.1062097
    • Götz J, Chen F, van Dorpe R, Nitsch RM. 2001. Formation of neurobrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils. Science 293:1491-1495. (Pubitemid 32807681)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 71
    • 0037439642 scopus 로고    scopus 로고
    • Aberrant activation of focal adhesion proteins mediates fibrillar amyloid β-induced neuronal dystrophy
    • Grace EA, Busciglio J. 2003. Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy. J Neurosci 23:493-502. (Pubitemid 36139548)
    • (2003) Journal of Neuroscience , vol.23 , Issue.2 , pp. 493-502
    • Grace, E.A.1    Busciglio, J.2
  • 72
    • 0037130570 scopus 로고    scopus 로고
    • Characterization of neuronal dystrophy induced by fibrillar amyloid β: Implications for Alzheimer's disease
    • DOI 10.1016/S0306-4522(02)00241-5, PII S0306452202002415
    • Grace EA, Rabiner CA, Busciglio J. 2002. Characterization of neuronal dystrophy induced by fibrillar amyloid beta: implications for Alzheimer's disease. Neuroscience 114:265-273. (Pubitemid 35247506)
    • (2002) Neuroscience , vol.114 , Issue.1 , pp. 265-273
    • Grace, E.A.1    Rabiner, C.A.2    Busciglio, J.3
  • 74
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation on tau: Generation of paired helical filament epitopes and neuronal localization of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. 1992. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation on tau: generation of paired helical filament epitopes and neuronal localization of the kinase. Neurosci Lett 147:58-62.
    • (1992) Neurosci Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 75
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J, Selkoe DJ. 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 76
    • 44549088952 scopus 로고    scopus 로고
    • Parkinson's disease and pesticides: A toxicological perspective
    • Hatcher JM, Pennell KD, Miller GW. 2008. Parkinson's disease and pesticides: a toxicological perspective. Trends Pharmacol Sci 29:322-329.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 322-329
    • Hatcher, J.M.1    Pennell, K.D.2    Miller, G.W.3
  • 77
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- And F- actin
    • DOI 10.1021/bi00089a015
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR. 1993. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32:9994-10004. (Pubitemid 23312425)
    • (1993) Biochemistry , vol.32 , Issue.38 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 78
    • 33745780575 scopus 로고    scopus 로고
    • Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid β-induced degeneration: A potential mechanism of neuronal dystrophy in Alzheimer's disease
    • DOI 10.1523/JNEUROSCI.5567-05.2006
    • Heredia L, Helguera P, de Olmos S, Kedikian G, Sola VF, LaFerla F, Staufenbiel M, de Olmos J, Busciglio J, Caceres A, Lorenzo A. 2006. Phosphorylation of actin-depolymerizing factor/cofilin by LIM-kinase mediates amyloid beta-induced degeneration: a potential mechanism of neuronal dystrophy in Alzheimer's disease. J Neurosci 26:6533-6542. (Pubitemid 44318334)
    • (2006) Journal of Neuroscience , vol.26 , Issue.24 , pp. 6533-6542
    • Heredia, L.1    Helguera, P.2    De Olmos, S.3    Kedikian, G.4    Vigo, F.S.5    Laferla, F.6    Staufenbiel, M.7    De Olmos, J.8    Busciglio, J.9    Caceres, A.10    Lorenzo, A.11
  • 79
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • Himmler A. 1989. Structure of the tau gene: alternatively spliced transcripts generate a protein family. Mol Cell Biol 9:1389-1396. (Pubitemid 19095178)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.4 , pp. 1389-1396
    • Himmler, A.1
  • 80
    • 0028286860 scopus 로고
    • Hirano bodies and related neuronal inclusions
    • Hirano A. 1994. Hirano bodies and related neuronal inclusions. Neuropathol Appl Neurobiol 20:3-11. (Pubitemid 24078160)
    • (1994) Neuropathology and Applied Neurobiology , vol.20 , Issue.1 , pp. 3-11
    • Hirano, A.1
  • 81
    • 0014276827 scopus 로고
    • The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex
    • Hirano A, Dembitzer HM, Kurland LT, Zimmerman HM. 1968. The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex. J Neuropathol Exp Neurol 27:167-182.
    • (1968) J Neuropathol Exp Neurol , vol.27 , pp. 167-182
    • Hirano, A.1    Dembitzer, H.M.2    Kurland, L.T.3    Zimmerman, H.M.4
  • 82
    • 0141864562 scopus 로고    scopus 로고
    • Glutamate and amyloid β-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms
    • Hiruma H, Katakura T, Takahashi S, Ichikawa T, Kawakami T. 2003. Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J Neurosci 23:8967-8977. (Pubitemid 37210910)
    • (2003) Journal of Neuroscience , vol.23 , Issue.26 , pp. 8967-8977
    • Hiruma, H.1    Katakura, T.2    Takahashi, S.3    Ichikawa, T.4    Kawakami, T.5
  • 83
    • 40249097516 scopus 로고    scopus 로고
    • The Subspine Organization of Actin Fibers Regulates the Structure and Plasticity of Dendritic Spines
    • DOI 10.1016/j.neuron.2008.01.013, PII S0896627308000743
    • Honkura N, Matsuzaki M, Noguchi J, Ellis-Davies GC, Kasai H. 2008. The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57:719-729. (Pubitemid 351335344)
    • (2008) Neuron , vol.57 , Issue.5 , pp. 719-729
    • Honkura, N.1    Matsuzaki, M.2    Noguchi, J.3    Ellis-Davies, G.C.R.4    Kasai, H.5
  • 84
    • 55549091059 scopus 로고    scopus 로고
    • Chronophin mediates an ATP-sensing mechanism of cofilin dephosphorylation and neuronal cofilin-actin rod formation
    • Huang TY, Minamide LS, Bamburg JR, Bokoch GM. 2008. Chronophin mediates an ATP-sensing mechanism of cofilin dephosphorylation and neuronal cofilin-actin rod formation. Dev Cell 15:691-703.
    • (2008) Dev Cell , vol.15 , pp. 691-703
    • Huang, T.Y.1    Minamide, L.S.2    Bamburg, J.R.3    Bokoch, G.M.4
  • 85
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung LW, Ciccotosto GD, Giannakis E, Tew DJ, Perez K, Masters CL, Cappai R, Wade JD, Barnham KJ. 2008. Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: abeta dimers and trimers correlate with neurotoxicity. J Neurosci 28:11950-11958.
    • (2008) J Neurosci , vol.28 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3    Tew, D.J.4    Perez, K.5    Masters, C.L.6    Cappai, R.7    Wade, J.D.8    Barnham, K.J.9
  • 86
    • 0028899724 scopus 로고
    • Quantitative analysis of senile plaques in Alzheimer disease: Observation of log-normal size distribution and molecular epidemiology of differences associated with apolpoprotein e geneotype and trisomy 21 (Down syndrome)
    • Hyman BT, Weat HL, Rebeck GW, Buldyrev SV, Mantegna RN, Ukleja M, Havlin S, Stanley HE. 1995. Quantitative analysis of senile plaques in Alzheimer disease: observation of log-normal size distribution and molecular epidemiology of differences associated with apolpoprotein E geneotype and trisomy 21 (Down syndrome). Proc Natl Acad Sci USA 92:3586-3590.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3586-3590
    • Hyman, B.T.1    Weat, H.L.2    Rebeck, G.W.3    Buldyrev, S.V.4    Mantegna, R.N.5    Ukleja, M.6    Havlin, S.7    Stanley, H.E.8
  • 87
    • 0022517773 scopus 로고
    • Reversible induction of actin rods in mouse C3H-2K cells by incubation in salt buffers and by treatment with non-ionic detergents
    • Iida K, Yahara I. 1986. Reversible induction of actin rods in mouse C3H-2K cells by incubation in salt buffers and by treatment with non-ionic detergents. Exp Cell Res 164:492-506. (Pubitemid 16042094)
    • (1986) Experimental Cell Research , vol.164 , Issue.2 , pp. 492-506
    • Iida, K.1    Yahara, I.2
  • 88
    • 0022510684 scopus 로고
    • Heat shock induction of intranuclear actin rods in cultured mammalian cells
    • Iida K, Iida H, Yahara I. 1986. Heat shock induction of intranuclear actin rods in cultured mammalian cells. Exp Cell Res 165:207-215. (Pubitemid 16072272)
    • (1986) Experimental Cell Research , vol.165 , Issue.1 , pp. 207-215
    • Iida, K.1    Iida, H.2    Yahara, I.3
  • 89
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida K, Matsumoto S, Yahara I. 1992. The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct 17:39-46.
    • (1992) Cell Struct Funct , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 91
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • DOI 10.1016/S0014-5793(96)01386-5, PII S0014579396013865
    • Kampers T, Friedhoff P, Biernat J, Mandelkow EM. 1996. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399:344-349. (Pubitemid 26426879)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 92
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of Tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova I, Biernat J, Wang Y, Pickhardt M, von Bergen M, Gazova Z, Mandelkow E, Mandelkow EM. 2006. Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J Biol Chem 281:1205-1214.
    • (2006) J Biol Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    Von Bergen, M.5    Gazova, Z.6    Mandelkow, E.7    Mandelkow, E.M.8
  • 93
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • Kidd M. 1963. Paired helical filaments in electron microscopy of Alzheimer's disease. Nature 197:192-193.
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 94
    • 0033539689 scopus 로고    scopus 로고
    • Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression
    • King ME, Ahuja V, Binder LI, Kuret J. 1999. Ligand-dependent tau filament formation: implications for Alzheimer's disease progression. Biochem 38:14851-14859. (Pubitemid 129517629)
    • (1999) Biochemistry , vol.38 , Issue.45 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 95
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
    • DOI 10.1083/jcb.200605187
    • King ME, Kan H-M, Baas PW, Erisir A, Glabe CG, Bloom GS. 2006. Tau-dependent microtubule disassembly initiated by pre-fibrillar β-amyloid. J Cell Biol 175:541-546. (Pubitemid 44790607)
    • (2006) Journal of Cell Biology , vol.175 , Issue.4 , pp. 541-546
    • King, M.E.1    Kan, H.-M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5    Bloom, G.S.6
  • 96
    • 34247632141 scopus 로고    scopus 로고
    • Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: A study of neurological disorders accompanied by cognitive deficits
    • DOI 10.1016/j.neures.2007.02.003, PII S0168010207000582
    • Kojima N, Shirao T. 2007. Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. Neurosci Res 58:1-5. (Pubitemid 46678494)
    • (2007) Neuroscience Research , vol.58 , Issue.1 , pp. 1-5
    • Kojima, N.1    Shirao, T.2
  • 98
    • 0021739339 scopus 로고
    • Microtubule-associated protein 2: Monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles
    • Kosik KS, Duffy LK, Dowling MM, Abraham C, McCluskey A, Selkoe DJ. 1984. Microtubule-associated protein 2: monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles. Proc Natl Acad Sci USA 81:7941-7945.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7941-7945
    • Kosik, K.S.1    Duffy, L.K.2    Dowling, M.M.3    Abraham, C.4    McCluskey, A.5    Selkoe, D.J.6
  • 103
    • 0031765270 scopus 로고    scopus 로고
    • Glutamate toxicity in chronic neurodegenerative disease
    • Lancelot E, Beal MF. 1998. Glutamate toxicity in chronic neurodegenerative disease. Prog Brain Res 116:331-347. (Pubitemid 28526944)
    • (1998) Progress in Brain Research , vol.116 , pp. 331-347
    • Lancelot, E.1    Beal, M.F.2
  • 104
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G, Cowan N, Kirschner M. 1988. The primary structure and heterogeneity of Tau protein from mouse brain. Science 239:285-288. (Pubitemid 18061495)
    • (1988) Science , vol.239 , Issue.4837 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 107
    • 3142704290 scopus 로고    scopus 로고
    • Novel isoforms of tau that lack the microtubule-binding domain
    • DOI 10.1111/j.1471-4159.2004.02508.x
    • Luo MH, Tse SW, Memmott J, Andreadis A. 2004. Novel isoforms of tau that lack the microtubule-binding domain. J Neurochem 90:340-351. (Pubitemid 38938220)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.2 , pp. 340-351
    • Luo, M.-H.1    Tse, S.-W.2    Memmott, J.3    Andreadis, A.4
  • 108
    • 0028803993 scopus 로고
    • Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies
    • Maciver SK, Harrington CR. 1995. Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies. Neuroreport 6:1985-1988.
    • (1995) Neuroreport , vol.6 , pp. 1985-1988
    • Maciver, S.K.1    Harrington, C.R.2
  • 109
    • 34347347236 scopus 로고    scopus 로고
    • Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies
    • Maloney MT, Bamburg JR. 2007. Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies. Mol Neurobiol 35:21-44.
    • (2007) Mol Neurobiol , vol.35 , pp. 21-44
    • Maloney, M.T.1    Bamburg, J.R.2
  • 110
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: A feedforward mechanism for Alzheimer's disease
    • Maloney MT, Minamide LS, Kinley AW, Boyle JA, Bamburg JR. 2005. Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer's disease. J Neurosci 25:11313-11321.
    • (2005) J Neurosci , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 111
    • 0026619584 scopus 로고
    • Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau
    • DOI 10.1016/0014-5793(92)81496-9
    • Mandelkow EM, Drewes G, Biernat J, Gustke N, Van Lint J, Vandenheede JR, Mandelkow E. 1992. Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau. FEBS Lett 314:315-321. (Pubitemid 23005680)
    • (1992) FEBS Letters , vol.314 , Issue.3 , pp. 315-321
    • Mandelkow, E.-M.1    Drewes, G.2    Biernat, J.3    Gustke, N.4    Van Lint, J.5    Vandenheede, J.R.6    Mandelkow, E.7
  • 112
    • 0021264594 scopus 로고
    • Alzheimer's presenile dementia, senile dementia of Alzheimer type and Down's syndrome in middle age from an age related continuum of pathological changes
    • Mann DM, Yates PO, Marcyniuk B. 1984. Alzheimer's presenile dementia, senile dementia of Alzheimer type and Down's syndrome in middle age form an age related continuum of pathological changes. Neuropathol Appl Neurobiol 10:185-207. (Pubitemid 14121330)
    • (1984) Neuropathology and Applied Neurobiology , vol.10 , Issue.3 , pp. 185-207
    • Mann, D.M.A.1    Yates, P.O.2    Marcyniuk, B.3
  • 113
  • 114
    • 0036573221 scopus 로고    scopus 로고
    • Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein
    • Maselli AG, Davis R, Thomson SAM, Davis RC, Fechheimer M. 2002. Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein. J Cell Sci 115:1939-1949. (Pubitemid 34567255)
    • (2002) Journal of Cell Science , vol.115 , Issue.9 , pp. 1939-1952
    • Maselli, A.G.1    Davis, R.2    Furukawa, R.3    Fechheimer, M.4
  • 115
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • DOI 10.1038/nature02621
    • Mattson MP. 2004. Pathways towards and away from Alzheimer's disease. Nature 430:631-639. (Pubitemid 39061671)
    • (2004) Nature , vol.430 , Issue.7000 , pp. 631-639
    • Mattson, M.P.1
  • 116
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • DOI 10.1083/jcb.138.4.771
    • McGough A, Pope B, Chiu W, Weeds A. 1997. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol 138:771-781. (Pubitemid 27365041)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 117
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • DOI 10.1002/(SICI)1097-0169(1998)39:2<172::AID-CM8>3.0.CO;2-8
    • Meberg PJ, Ono S, Minamide LS, Takahashi M, Bamburg JR. 1998. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil Cytoskeleton 39:172-190. (Pubitemid 28079648)
    • (1998) Cell Motility and the Cytoskeleton , vol.39 , Issue.2 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 118
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR. 2000. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2:628-636.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 121
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K, Iida K, Yahara I. 1996. Phosphorylation of ser-3 of cofilin regulates its essential function on actin. Genes Cells 1:73-86. (Pubitemid 126673108)
    • (1996) Genes to Cells , vol.1 , Issue.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 123
    • 0024449354 scopus 로고
    • Loss of nerve growth factor receptor-containing neurons in Alzheimer's disease: A quantitative analysis across subregions of the basal forebrain
    • DOI 10.1016/0014-4886(89)90124-6
    • Mufson EJ, Bothwell M, Kordower JH. 1989. Loss of nerve growth factor receptor-containing neurons in Alzheimer's disease: a quantitative analysis across subregions of the basal forebrain. Exp Neurol 105:221-232. (Pubitemid 19232573)
    • (1989) Experimental Neurology , vol.105 , Issue.3 , pp. 221-232
    • Mufson, E.J.1    Bothwell, M.2    Kordower, J.H.3
  • 124
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell J, Farlow M, Ghetti B, Benson MD. 1991. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 254:97-99. (Pubitemid 21917324)
    • (1991) Science , vol.254 , Issue.5028 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 125
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • DOI 10.1016/0169-328X(86)90033-1
    • Neve RL, Harris P, Kosik KS, Kurnit DM, Donlon TA. 1986. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of genes for tau and microtubule-associated protein 2. Mol Brain Res 1:271-280. (Pubitemid 17220131)
    • (1986) Molecular Brain Research , vol.1 , Issue.3 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3
  • 126
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H. 1987. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 84:5262-5266.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 127
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • DOI 10.1016/S0092-8674(01)00638-9
    • Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108:233-246. (Pubitemid 34161143)
    • (2002) Cell , vol.108 , Issue.2 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 128
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M, Kabat J, Wischik CM. 1993. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J 12:365-370. (Pubitemid 23042416)
    • (1993) EMBO Journal , vol.12 , Issue.1 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 129
    • 0022723508 scopus 로고
    • One of the antigenic determinants of paired helical filaments is related to tau protein
    • Nukina N, Ihara Y. 1986. One of the antigenic determinants of paired helical filaments is related to tau protein. J Biochem 99:1541-1544.
    • (1986) J Biochem , vol.99 , pp. 1541-1544
    • Nukina, N.1    Ihara, Y.2
  • 130
    • 0029928003 scopus 로고    scopus 로고
    • Apolipoprotein e polymorphism and susceptibility to early- And late-onset sporadic Alzheimer's disease in Hokkaido, the northern part of Japan
    • DOI 10.1016/0304-3940(96)12415-0
    • Nunomura A, Chiba S, Eto M, Saito M, Makino I, Miyagishi T. 1996. Apolipoprotein E polymorphism and susceptibility to early- and late-onset sproadic Alzheimer's disease in Hokkaido, the northern part of Japan. Neurosci Lett 206:17-20. (Pubitemid 26084719)
    • (1996) Neuroscience Letters , vol.206 , Issue.1 , pp. 17-20
    • Nunomura, A.1    Chiba, S.2    Eto, M.3    Saito, M.4    Makino, I.5    Miyagishi, T.6
  • 132
    • 0024429070 scopus 로고
    • Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin
    • Ohta Y, Nishida E, Sakai H, Miyamoto E. 1989. Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J Biol Chem 264:16143-16148. (Pubitemid 19238376)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.27 , pp. 16143-16148
    • Ohta, Y.1    Nishida, E.2    Sakai, H.3    Miyamoto, E.4
  • 134
    • 0024241030 scopus 로고
    • High molecular weight microtubule-associated proteins bind to actin lattices (Hirano bodies)
    • Peterson C, Kress Y, Valle R, Goldman JE. 1988. High molecular weight microtubule-associated proteins bind to actin lattices (Hirano bodies). Acta Neuropathol (Berl) 77:168-174. (Pubitemid 19015554)
    • (1988) Acta Neuropathologica , vol.77 , Issue.2 , pp. 168-174
    • Peterson, C.1    Kress, Y.2    Vallee, R.3    Goldman, J.E.4
  • 135
    • 0030913980 scopus 로고    scopus 로고
    • The 'jaws' model of tau-microtubule interaction examined in CHO cells
    • Preuss U, Biernat J, Mandelkow EM, Mandelkow E. 1997. The jaws model of tau-microtubule interaction examined in CHO cells. J Cell Sci 110 (Part 6):789-800. (Pubitemid 27156328)
    • (1997) Journal of Cell Science , vol.110 , Issue.6 , pp. 789-800
    • Preuss, U.1    Biernat, J.2    Mandelkow, E.-M.3    Mandelkow, E.4
  • 136
  • 138
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • DOI 10.1126/science.1141736
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T, Gerstein H, Yu GQ, Mucke L. 2007. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316:750-754. (Pubitemid 46717684)
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.-Q.8    Mucke, L.9
  • 140
    • 0024393482 scopus 로고
    • Analysis of epitopes shared by Hirano bodies and neurofilament proteins in normal and Alzheimer's disease hippocampus
    • Schmidt ML, Lee VM, Trojanowsk JQ. 1989. Analysis of epitopes shared by Hirano bodies and neurofilament proteins in normal and Alzheimer's disease hippocampus. Lab Invest 60:513-522.
    • (1989) Lab Invest , vol.60 , pp. 513-522
    • Schmidt, M.L.1    Lee, V.M.2    Trojanowsk, J.Q.3
  • 142
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL. 2007. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27:2866-2875. (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 144
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • DOI 10.1016/S0304-3940(02)00210-0, PII S0304394002002100
    • Shim KS, Lubec G. 2002. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci Lett 324:209-212. (Pubitemid 34493871)
    • (2002) Neuroscience Letters , vol.324 , Issue.3 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 145
    • 0028985799 scopus 로고
    • Role of the beta-amyloid protein in Alzheimer's disease
    • Sisodia SS, Price DL. 1995. Role of the beta-amyloid protein in Alzheimer's disease. FASEB J 9:366-370.
    • (1995) FASEB J , vol.9 , pp. 366-370
    • Sisodia, S.S.1    Price, D.L.2
  • 146
    • 0034941330 scopus 로고    scopus 로고
    • Nerve growth factor signaling, neuroprotection, and neural repair
    • DOI 10.1146/annurev.neuro.24.1.1217
    • Sofroniew MV, Howe CL, Mobley WC. 2001. Nerve growth factor signaling, neuroprotection, and neural repair. Annu Rev Neurosci 24:1217-1281. (Pubitemid 32695259)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 1217-1281
    • Sofroniew, M.V.1    Howe, C.L.2    Mobley, W.C.3
  • 147
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A
    • DOI 10.1016/S0896-6273(00)80250-0
    • Sontag E, Nunbhakdi-Craig V, Lee G, Bloom GS, Mumby MC. 1996. Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A. Neuron 17:1201-1207. (Pubitemid 27021104)
    • (1996) Neuron , vol.17 , Issue.6 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 148
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules: Implications for the regulation of tau phosphorylation and the development of tauopathies
    • Sontag E, Nunbhakdi-Craig V, Lee G, Brandt R, Kamibayashi C, Kuret J, White CL, III, Mumby MC, Bloom GS. 1999. Molecular interactions among protein phosphatase 2A, tau and microtubules: implications for the regulation of tau phosphorylation and the development of tauopathies. J Biol Chem 274:25490-25498. (Pubitemid 129530718)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.36 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6    White III, C.L.7    Mumby, M.C.8    Bloom, G.S.9
  • 151
    • 33746572249 scopus 로고    scopus 로고
    • Increased BACE1 maturation contributes to the pathogenesis of Alzheimer's disease in Down syndrome
    • DOI 10.1096/fj.05-5628com
    • Sun X, Tong Y, Qing H, Chen CH, Song W. 2006a. Increased BACE1 maturation contributes to the pathogenesis of Alzheimer's disease in Down syndrome. FASEB J 20:1361-1368. (Pubitemid 44943844)
    • (2006) FASEB Journal , vol.20 , Issue.9 , pp. 1361-1368
    • Sun, X.1    Tong, Y.2    Qing, H.3    Chen, C.-H.4    Song, W.5
  • 152
    • 33746549926 scopus 로고    scopus 로고
    • BACE2, as a novel APP θ-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome
    • DOI 10.1096/fj.05-5632com
    • Sun X, He G, Song W. 2006b. BACE2 as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome. FASEB J 20:1369-1376. (Pubitemid 44943845)
    • (2006) FASEB Journal , vol.20 , Issue.9 , pp. 1369-1376
    • Sun, X.1    He, G.2    Song, W.3
  • 153
    • 0033836580 scopus 로고    scopus 로고
    • In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification
    • Takeda A, Smith MA, Avila J, Nunomura A, Siedlak SL, Zhu X, Perry G, Sayre LM. 2000. In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification. J Neurochem 75:1234-1241.
    • (2000) J Neurochem , vol.75 , pp. 1234-1241
    • Takeda, A.1    Smith, M.A.2    Avila, J.3    Nunomura, A.4    Siedlak, S.L.5    Zhu, X.6    Perry, G.7    Sayre, L.M.8
  • 154
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • DOI 10.1016/j.cell.2005.02.008
    • Tanzi RE, Bertram L. 2005. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120:545-555. (Pubitemid 40269768)
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 155
    • 0016261927 scopus 로고
    • Ultrastructure of Hirano bodies
    • Berl
    • Tomonaga M. 1974. Ultrastructure of Hirano bodies. Acta Neuropathol (Berl) 28:365-366.
    • (1974) Acta Neuropathol , vol.28 , pp. 365-366
    • Tomonaga, M.1
  • 156
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima J, Toshima JY, Amano T, Yang N, Narumiya S, Mizuno K. 2001. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganzation and focal adhesion formation. Mol Biol Cell 12:1131-1145. (Pubitemid 33052004)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 157
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signaling
    • Turner CE. 2000. Paxillin and focal adhesion signaling. Nat Cell Biol 2:E231-E236.
    • (2000) Nat Cell Biol , vol.2
    • Turner, C.E.1
  • 158
    • 0019824177 scopus 로고
    • Axonal transport: Each major rate component reflects the movement of distinct macromolecular complexes
    • Tytell M, Black MM, Garner JA, Lasek RJ. 1981. Axonal transport: each of the major rate components consist of distinct macromolecular complexes. Science 214:179-181. (Pubitemid 12243412)
    • (1981) Science , vol.214 , Issue.4517 , pp. 179-181
    • Tytell, M.1    Black, M.M.2    Garner, J.A.3    Lasek, R.J.4
  • 159
    • 0032495144 scopus 로고    scopus 로고
    • Striation is the characteristic neuritic abnormality in Alzheimer disease
    • DOI 10.1016/S0006-8993(98)01034-8, PII S0006899398010348
    • Velasco ME, Smith MA, Siedlak SL, Nunomura A, Perry G. 1998. Striation is the characteristic abnormality in Alzheimer disease. Brain Res 813:329-333. (Pubitemid 29009649)
    • (1998) Brain Research , vol.813 , Issue.2 , pp. 329-333
    • Velasco, M.E.1    Smith, M.A.2    Siedlak, S.L.3    Nunomura, A.4    Perry, G.5
  • 160
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ. 2002. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416:535-539. (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 163
    • 34347374867 scopus 로고    scopus 로고
    • BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin
    • DOI 10.1083/jcb.200703055
    • Wen Z, Han L, Bamburg JR, Shim S, Ming GL, Zheng JQ. 2007. BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin. J Cell Biol 178:107-119. (Pubitemid 47026406)
    • (2007) Journal of Cell Biology , vol.178 , Issue.1 , pp. 107-119
    • Wen, Z.1    Han, L.2    Bamburg, J.R.3    Shim, S.4    Ming, G.-L.5    Zheng, J.Q.6
  • 165
    • 67749086394 scopus 로고    scopus 로고
    • Mitochondrial dysfuction induces the accumulation of microtubule- associated protein in Alzheimer-like striated neurites
    • Abstract 1069
    • Whiteman IT, Cullen KM, Antao ST, Witting PK, Bamburg JR, Goldsbury C. 2008. Mitochondrial dysfuction induces the accumulation of microtubule- associated protein in Alzheimer-like striated neurites. Mol Biol Cell 19 (Suppl): Abstract 1069.
    • (2008) Mol Biol Cell , vol.19 , Issue.SUPPL.
    • Whiteman, I.T.1    Cullen, K.M.2    Antao, S.T.3    Witting, P.K.4    Bamburg, J.R.5    Goldsbury, C.6
  • 166
    • 0028826633 scopus 로고
    • Polymerization of microtubule-associated protein tau under near-physiological conditions
    • Wilson DM, Binder LI. 1995. Polymerization of microtubule-associated protein tau under near-physiological conditions. J Biol Chem 270:24306-24314.
    • (1995) J Biol Chem , vol.270 , pp. 24306-24314
    • Wilson, D.M.1    Binder, L.I.2
  • 167
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid β peptides
    • Wilson DM, Binder LI. 1997. Free fatty acids stimulate the polymerization of tau and amyloid β peptides. Am J Pathol 150:2181-2195.
    • (1997) Am J Pathol , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 168
    • 0021796959 scopus 로고
    • Subunit structure of paired helical filaments in Alzheimer's disease
    • DOI 10.1083/jcb.100.6.1905
    • Wischik CM, Crowther RA, Stewart M, Roth M. 1985. Subunit structure of paired helical filaments in Alzheimer's disease. J Cell Biol 100:1905-1912. (Pubitemid 15042085)
    • (1985) Journal of Cell Biology , vol.100 , Issue.6 , pp. 1905-1912
    • Wischik, C.M.1    Crowther, R.A.2    Stewart, M.3    Roth, M.4
  • 170
    • 0029057814 scopus 로고
    • Intracellular a beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang AJ, Knauer M, Burdick DA, Glabe C. 1995. Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J Biol Chem 270:14786-14792.
    • (1995) J Biol Chem , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 171
    • 0032565769 scopus 로고    scopus 로고
    • Cofflin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • DOI 10.1038/31735
    • Yang N, Higuchi O, Ohashi K, Nagata K, Wada A, Kangawa K, Nishida E, Mizuno K. 1998. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393:809-812. (Pubitemid 28299495)
    • (1998) Nature , vol.393 , Issue.6687 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8
  • 174
    • 64249129005 scopus 로고    scopus 로고
    • Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimer's disease
    • Zhao WQ, Townsend M. 2009. Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimer's disease. Biochim Biophys Acta 1792:482-496.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 482-496
    • Zhao, W.Q.1    Townsend, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.