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Volumn 3, Issue 6, 2011, Pages 1-25

Biochemistry and cell biology of Tau protein in neurofibrillary degeneration

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 84863871956     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a006247     Document Type: Review
Times cited : (17)

References (252)
  • 1
    • 0021681351 scopus 로고
    • Microtubule-associated proteins connect microtubules and neurofilaments in vitro
    • Aamodt EJ, Williams RC Jr. 1984. Microtubule-associated proteins connect microtubules and neurofilaments in vitro. Biochemistry 23: 6023-6031.
    • (1984) Biochemistry , vol.23 , pp. 6023-6031
    • Aamodt, E.J.1    Williams Jr., R.C.2
  • 2
    • 0034730759 scopus 로고    scopus 로고
    • Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
    • Ackmann M, Wiech H, Mandelkow E. 2000. Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation. J Biol Chem 275: 30335-30343.
    • (2000) J Biol Chem , vol.275 , pp. 30335-30343
    • Ackmann, M.1    Wiech, H.2    Mandelkow, E.3
  • 3
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L. 2009. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64: 783-790.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 5
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J, Ozer RS, Safer D, Halpain S, Milligan RA. 2002. MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J Cell Biol 157: 1187-1196.
    • (2002) J Cell Biol , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 6
    • 39049193314 scopus 로고    scopus 로고
    • Misregulation of tau alternative splicing in neurodegeneration and dementia
    • Andreadis A. 2006. Misregulation of tau alternative splicing in neurodegeneration and dementia. Prog Mol Subcell Biol 44: 89-107.
    • (2006) Prog Mol Subcell Biol , vol.44 , pp. 89-107
    • Andreadis, A.1
  • 7
    • 0036798495 scopus 로고    scopus 로고
    • Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules
    • Aronov S, Aranda G, Behar L, Ginzburg I. 2002. Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules. J Cell Sci 115: 3817-3827.
    • (2002) J Cell Sci , vol.115 , pp. 3817-3827
    • Aronov, S.1    Aranda, G.2    Behar, L.3    Ginzburg, I.4
  • 8
    • 56749104288 scopus 로고    scopus 로고
    • Inclusion-body myositis: Muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains
    • Askanas V, Engel WK. 2008. Inclusion-body myositis: Muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol 116: 583-595.
    • (2008) Acta Neuropathol , vol.116 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 9
    • 0346120162 scopus 로고    scopus 로고
    • Slow axonal transport and the genesis of neuronal morphology
    • Baas PW, Buster DW. 2004. Slow axonal transport and the genesis of neuronal morphology. J Neurobiol 58: 3-17.
    • (2004) J Neurobiol , vol.58 , pp. 3-17
    • Baas, P.W.1    Buster, D.W.2
  • 10
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ. 2007. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8: 663-672.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 12
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain
    • Barghorn S, Davies P, MandelkowE. 2004. Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain. Biochemistry 43: 1694-1703.
    • (2004) Biochemistry , vol.43 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 13
    • 0023875705 scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. J Biol Chem 263: 5876-5883.
    • (1988) J Biol Chem , vol.263 , pp. 5876-5883
    • Baudier, J.1    Cole, R.D.2
  • 14
    • 0023190008 scopus 로고
    • Comparison of S100b protein with calmodulin: Interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C
    • Baudier J, Mochly-Rosen D, Newton A, Lee SH, Koshland DE Jr, Cole RD. 1987. Comparison of S100b protein with calmodulin: Interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C. Biochemistry 26: 2886-2893.
    • (1987) Biochemistry , vol.26 , pp. 2886-2893
    • Baudier, J.1    Mochly-Rosen, D.2    Newton, A.3    Lee, S.H.4    Koshland Jr., D.E.5    Cole, R.D.6
  • 15
    • 53149103944 scopus 로고    scopus 로고
    • Truncated Tau with the Fynbinding domain and without the microtubule-binding domain hinders the myelinating capacity of an oligodendrocyte cell line
    • Belkadi A, LoPresti P. 2008. Truncated Tau with the Fynbinding domain and without the microtubule-binding domain hinders the myelinating capacity of an oligodendrocyte cell line. J Neurochem 107: 351-360.
    • (2008) J Neurochem , vol.107 , pp. 351-360
    • Belkadi, A.1    LoPresti, P.2
  • 16
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure
    • Berriman J, Serpell LC, Oberg KA, Fink AL, Goedert M, Crowther RA. 2003. Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure. Proc Natl Acad Sci 100: 9034-9038.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 9034-9038
    • Berriman, J.1    Serpell, L.C.2    Oberg, K.A.3    Fink, A.L.4    Goedert, M.5    Crowther, R.A.6
  • 17
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and Tau
    • Bhaskar K, Yen SH, Lee G. 2005. Disease-related modifications in tau affect the interaction between Fyn and Tau. J Biol Chem 280: 35119-35125.
    • (2005) J Biol Chem , vol.280 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 19
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J, Gustke N, Drewes G, Mandelkow EM, Mandelkow E. 1993. Phosphorylation of Ser262 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
  • 21
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder LI, Frankfurter A, Rebhun LI. 1985. The distribution of tau in the mammalian central 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
  • 23
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. 1991. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82: 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 24
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E, Braak H, Mandelkow EM. 1994. A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol 87: 554-567.
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 25
    • 0028364256 scopus 로고
    • Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation
    • Brandt R, Lee G, Teplow DB, Shalloway D, Abdel-Ghany M. 1994. Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation. J Biol Chem 269: 11776-11782.
    • (1994) J Biol Chem , vol.269 , pp. 11776-11782
    • Brandt, R.1    Lee, G.2    Teplow, D.B.3    Shalloway, D.4    Abdel-Ghany, M.5
  • 26
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's aminoterminal projection domain
    • Brandt R, Leger J, Lee G. 1995. Interaction of tau with the neural plasma membrane mediated by tau's aminoterminal 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
  • 27
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models
    • Brandt R, Hundelt M, Shahani N. 2005. Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models. Biochim Biophys Acta 1739: 331-354.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 30
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner KA, Kirschner MW. 1991. Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 115: 717-730.
    • (1991) J Cell Biol , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 31
    • 1442324853 scopus 로고    scopus 로고
    • In vitro cultured neurons for molecular studies correlating apoptosis with events related to Alzheimer disease
    • Canu N, Calissano P. 2003. In vitro cultured neurons for molecular studies correlating apoptosis with events related to Alzheimer disease. Cerebellum 2: 270-278.
    • (2003) Cerebellum , vol.2 , pp. 270-278
    • Canu, N.1    Calissano, P.2
  • 32
    • 0034826896 scopus 로고    scopus 로고
    • Regulation of microtubuleassociated proteins
    • Cassimeris L, Spittle C. 2001. Regulation of microtubuleassociated proteins. Int Rev Cytol 210: 163-226.
    • (2001) Int Rev Cytol , vol.210 , pp. 163-226
    • Cassimeris, L.1    Spittle, C.2
  • 34
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen J, Kanai Y, Cowan NJ, Hirokawa N. 1992. Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 360: 674-677.
    • (1992) Nature , vol.360 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 35
    • 0038152836 scopus 로고    scopus 로고
    • Anionic micelles and vesicles induce tau fibrillization in vitro
    • Chirita CN, Necula M, Kuret J. 2003. Anionic micelles and vesicles induce tau fibrillization in vitro. J Biol Chem 278: 25644-25650.
    • (2003) J Biol Chem , vol.278 , pp. 25644-25650
    • Chirita, C.N.1    Necula, M.2    Kuret, J.3
  • 36
    • 17144395539 scopus 로고    scopus 로고
    • Triggers of full-length tau aggregation: A role for partially folded intermediates
    • Chirita CN, Congdon EE, Yin H, Kuret J. 2005. Triggers of full-length tau aggregation: A role for partially folded intermediates. Biochemistry 44: 5862-5872.
    • (2005) Biochemistry , vol.44 , pp. 5862-5872
    • Chirita, C.N.1    Congdon, E.E.2    Yin, H.3    Kuret, J.4
  • 37
    • 14544267623 scopus 로고    scopus 로고
    • 14-3-3 Protein mediates phosphorylation of microtubule-associated protein tau by serumand glucocorticoid-induced protein kinase 1
    • Chun J, Kwon T, Lee EJ, Kim CH, Han YS, Hong SK, Hyun S, Kang SS. 2004. 14-3-3 Protein mediates phosphorylation of microtubule-associated protein tau by serumand glucocorticoid-induced protein kinase 1. Mol Cells 18: 360-368.
    • (2004) Mol Cells , vol.18 , pp. 360-368
    • Chun, J.1    Kwon, T.2    Lee, E.J.3    Kim, C.H.4    Han, Y.S.5    Hong, S.K.6    Hyun, S.7    Kang, S.S.8
  • 39
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland DW, Hwo SY, KirschnerMW. 1977a. Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J Mol Biol 116: 227-247.
    • (1977) J Mol Biol , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 40
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland DW, Hwo SY, KirschnerMW. 1977b. Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J Mol Biol 116: 207-225.
    • (1977) J Mol Biol , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 42
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • Coleman PD, Yao PJ. 2003. Synaptic slaughter in Alzheimer's disease. Neurobiol Aging 24: 1023-1027.
    • (2003) Neurobiol Aging , vol.24 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 44
    • 0025977281 scopus 로고
    • Straight and paired helical filaments in Alzheimer disease have a common structural unit
    • Crowther RA. 1991. Straight and paired helical filaments in Alzheimer disease have a common structural unit. Proc Natl Acad Sci 88: 2288-2292.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 2288-2292
    • Crowther, R.A.1
  • 45
    • 0022435132 scopus 로고
    • Image reconstruction of the Alzheimer paired helical filament
    • Crowther RA, Wischik CM. 1985. Image reconstruction of the Alzheimer paired helical filament. EMBO J 4: 3661-3665.
    • (1985) EMBO J , vol.4 , pp. 3661-3665
    • Crowther, R.A.1    Wischik, C.M.2
  • 47
    • 0030998758 scopus 로고    scopus 로고
    • Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures
    • Davis DR, Anderton BH, Brion JP, Reynolds CH, Hanger DP. 1997. Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures. J Neurochem 68: 1590-1597.
    • (1997) J Neurochem , vol.68 , pp. 1590-1597
    • Davis, D.R.1    Anderton, B.H.2    Brion, J.P.3    Reynolds, C.H.4    Hanger, D.P.5
  • 48
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt L, Halpain S. 2005. The MAP2/Tau family of microtubule-associated proteins. Genome Biol 6: 204.
    • (2005) Genome Biol , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 50
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit R, Ross JL, Goldman YE, Holzbaur EL. 2008. Differential regulation of dynein and kinesin motor proteins by tau. Science 319: 1086-1089.
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 51
  • 52
    • 0027519666 scopus 로고
    • An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif
    • Doll T, Meichsner M, Riederer BM, Honegger P, Matus A. 1993. An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif. J Cell Sci 106: 633-639.
    • (1993) J Cell Sci , vol.106 , pp. 633-639
    • Doll, T.1    Meichsner, M.2    Riederer, B.M.3    Honegger, P.4    Matus, A.5
  • 53
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G, Ebneth A, PreussU, Mandelkow EM, Mandelkow E. 1997. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89: 297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 54
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • Drubin DG, Kirschner MW. 1986. Tau protein function in living cells. J Cell Biol 103: 2739-2746.
    • (1986) J Cell Biol , vol.103 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 56
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • Elbaum-Garfinkle S, Ramlall T, Rhoades E. 2010. The role of the lipid bilayer in tau aggregation. Biophys J 98: 2722-2730.
    • (2010) Biophys J , vol.98 , pp. 2722-2730
    • Elbaum-Garfinkle, S.1    Ramlall, T.2    Rhoades, E.3
  • 57
    • 37549025063 scopus 로고    scopus 로고
    • BAG-1 associates with Hsc70. Tau complex and regulates the proteasomal degradation of Tau protein
    • Elliott E, Tsvetkov P, Ginzburg I. 2007. BAG-1 associates with Hsc70. Tau complex and regulates the proteasomal degradation of Tau protein. J Biol Chem 282: 37276-37284.
    • (2007) J Biol Chem , vol.282 , pp. 37276-37284
    • Elliott, E.1    Tsvetkov, P.2    Ginzburg, I.3
  • 58
    • 80053031684 scopus 로고    scopus 로고
    • Systematic identification of tubulin interacting fragments of the microtubule-associated protein TAU leads to a highly efficient promoter of microtubule assembly
    • Fauquant C, Redeker V, Landrieu I, Wieruzseski JM, Verdegem D, Laprevote O, Lippens G, Gigant B, Knossow M. 2011. Systematic identification of tubulin interacting fragments of the microtubule-associated protein TAU leads to a highly efficient promoter of microtubule assembly. J Biol Chem 286: 33358-33368.
    • (2011) J Biol Chem , vol.286 , pp. 33358-33368
    • Fauquant, C.1    Redeker, V.2    Landrieu, I.3    Wieruzseski, J.M.4    Verdegem, D.5    Laprevote, O.6    Lippens, G.7    Gigant, B.8    Knossow, M.9
  • 59
    • 0017646208 scopus 로고
    • Microtubule assembly in vitro. Purification of assemblypromoting factors
    • Fellous A, Francon J, Lennon AM, Nunez J. 1977. Microtubule assembly in vitro. Purification of assemblypromoting factors. Eur J Biochem 78: 167-174.
    • (1977) Eur J Biochem , vol.78 , pp. 167-174
    • Fellous, A.1    Francon, J.2    Lennon, A.M.3    Nunez, J.4
  • 60
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff P, Schneider A, Mandelkow EM, Mandelkow E. 1998. Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry 37: 10223-10230.
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 61
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. 2009. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284: 12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 64
    • 0035140975 scopus 로고    scopus 로고
    • Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease
    • Garcia ML, Cleveland DW. 2001. Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease. Curr Opin Cell Biol 13: 41-48.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 41-48
    • Garcia, M.L.1    Cleveland, D.W.2
  • 65
    • 78449296170 scopus 로고    scopus 로고
    • Cleavage of Tau by calpain in Alzheimer's disease: The quest for the toxic 17 kD fragment
    • Garg S, Timm T, Mandelkow EM, Mandelkow E, Wang Y. 2011. Cleavage of Tau by calpain in Alzheimer's disease: The quest for the toxic 17 kD fragment. Neurobiol Aging 32: 1-14.
    • (2011) Neurobiol Aging , vol.32 , pp. 1-14
    • Garg, S.1    Timm, T.2    Mandelkow, E.M.3    Mandelkow, E.4    Wang, Y.5
  • 66
    • 0016344556 scopus 로고
    • Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules
    • Gaskin F, Cantor CR, Shelanski ML. 1974. Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J Mol Biol 89: 737-755.
    • (1974) J Mol Biol , vol.89 , pp. 737-755
    • Gaskin, F.1    Cantor, C.R.2    Shelanski, M.L.3
  • 68
    • 0034494233 scopus 로고    scopus 로고
    • Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments
    • Giannetti AM, Lindwall G, Chau MF, Radeke MJ, Feinstein SC, Kohlstaedt LA. 2000. Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments. Protein Sci 9: 2427-2435.
    • (2000) Protein Sci , vol.9 , pp. 2427-2435
    • Giannetti, A.M.1    Lindwall, G.2    Chau, M.F.3    Radeke, M.J.4    Feinstein, S.C.5    Kohlstaedt, L.A.6
  • 70
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M, Wischik CM, Crowther RA, Walker JE, Klug A. 1988. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau. Proc Natl Acad Sci 85: 4051-4055.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 71
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNAencoding 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. 1989. Cloning and sequencing of the cDNAencoding 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.
    • (1989) EMBO J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 72
    • 0026512915 scopus 로고
    • Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system
    • Goedert M, Spillantini MG, Crowther RA. 1992. Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Proc Natl Acad Sci 89: 1983-1987.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 1983-1987
    • Goedert, M.1    Spillantini, M.G.2    Crowther, R.A.3
  • 73
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M, Jakes R, Crowther RA, Cohen P, Vanmechelen E, Vandermeeren M, Cras P. 1994. Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein. Biochem J 301: 871-877.
    • (1994) Biochem J , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 74
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA. 1996. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383: 550-553.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 75
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M, Clavaguera F, Tolnay M. 2010. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci 33: 317-325.
    • (2010) Trends Neurosci , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 76
    • 84864383087 scopus 로고    scopus 로고
    • Frontotemporal dementia: Implications for understanding Alzheimer disease
    • doi: 10.1101/cshperspect.a006254
    • Goedert M, Ghetti B, Grazia Spillantini M. 2011. Frontotemporal dementia: Implications for understanding Alzheimer disease. Cold Spring Harb Perspect Med doi: 10.1101/cshperspect.a006254.
    • (2011) Cold Spring Harb Perspect Med
    • Goedert, M.1    Ghetti, B.2    Grazia Spillantini, M.3
  • 78
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode BL, Feinstein SC. 1994. Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau. JCell Biol 124: 769-782.
    • (1994) JCell Biol , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 79
    • 68849123079 scopus 로고    scopus 로고
    • Accumulation of tau induced in neurites by microglial proinflammatory mediators
    • Gorlovoy P, Larionov S, Pham TT, Neumann H. 2009. Accumulation of tau induced in neurites by microglial proinflammatory mediators. FASEB J 23: 2502-2513.
    • (2009) FASEB J , vol.23 , pp. 2502-2513
    • Gorlovoy, P.1    Larionov, S.2    Pham, T.T.3    Neumann, H.4
  • 80
    • 0036956875 scopus 로고    scopus 로고
    • Studying gene function in eukaryotes by conditional gene inactivation
    • Gossen M, Bujard H. 2002. Studying gene function in eukaryotes by conditional gene inactivation. Annu Rev Genet 36: 153-173.
    • (2002) Annu Rev Genet , vol.36 , pp. 153-173
    • Gossen, M.1    Bujard, H.2
  • 81
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • Gotz J, Ittner LM. 2008. Animal models of Alzheimer's disease and frontotemporal dementia. Nat Rev Neurosci 9: 532-544.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 84
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SG, Davies P. 1990. A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci 87: 5827-5831.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 85
    • 0018129689 scopus 로고
    • Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
    • Griffith LM, Pollard TD. 1978. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J Cell Biol 78: 958-965.
    • (1978) J Cell Biol , vol.78 , pp. 958-965
    • Griffith, L.M.1    Pollard, T.D.2
  • 86
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LI. 1986. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. ProcNatl Acad Sci 83: 4913-4917.
    • (1986) ProcNatl Acad Sci , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3    Quinlan, M.4    Wisniewski, H.M.5    Binder, L.I.6
  • 87
    • 0029843684 scopus 로고    scopus 로고
    • Tau is widely expressed in rat tissues
    • Gu Y, Oyama F, Ihara Y. 1996. Tau is widely expressed in rat tissues. J Neurochem 67: 1235-1244.
    • (1996) J Neurochem , vol.67 , pp. 1235-1244
    • Gu, Y.1    Oyama, F.2    Ihara, Y.3
  • 89
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C, Selkoe DJ. 2007. Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 91
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. 1992. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation 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
  • 93
    • 0036323447 scopus 로고    scopus 로고
    • MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction
    • Harada A, Teng J, Takei Y, Oguchi K, Hirokawa N. 2002. MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction. J Cell Biol 158: 541-549.
    • (2002) J Cell Biol , vol.158 , pp. 541-549
    • Harada, A.1    Teng, J.2    Takei, Y.3    Oguchi, K.4    Hirokawa, N.5
  • 94
    • 40849095902 scopus 로고    scopus 로고
    • The HapMap: Charting a course for genetic discovery in neurological diseases
    • Hardy J, Singleton A. 2008. The HapMap: Charting a course for genetic discovery in neurological diseases. ArchNeurol 65: 319-321.
    • (2008) ArchNeurol , vol.65 , pp. 319-321
    • Hardy, J.1    Singleton, A.2
  • 95
    • 33846203763 scopus 로고    scopus 로고
    • Hibernation model of tau phosphorylation in hamsters: Selective vulnerability of cholinergic basal forebrain neurons-Implications for Alzheimer's disease
    • Hartig W, Stieler J, Boerema AS, Wolf J, Schmidt U, Weissfuss J, Bullmann T, Strijkstra AM, Arendt T. 2007. Hibernation model of tau phosphorylation in hamsters: Selective vulnerability of cholinergic basal forebrain neurons-Implications for Alzheimer's disease. Eur J Neurosci 25: 69-80.
    • (2007) Eur J Neurosci , vol.25 , pp. 69-80
    • Hartig, W.1    Stieler, J.2    Boerema, A.S.3    Wolf, J.4    Schmidt, U.5    Weissfuss, J.6    Bullmann, T.7    Strijkstra, A.M.8    Arendt, T.9
  • 96
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3z is an effector of tau protein phosphorylation
    • Hashiguchi M, Sobue K, Paudel HK. 2000. 14-3-3z is an effector of tau protein phosphorylation. J Biol Chem 275: 25247-25254.
    • (2000) J Biol Chem , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 98
    • 0018149343 scopus 로고
    • Radioimmunoassay for tubulin: A quantitative comparison of the tubulin content of different established tissue culture cells and tissues
    • Hiller G, Weber K. 1978. Radioimmunoassay for tubulin: A quantitative comparison of the tubulin content of different established tissue culture cells and tissues. Cell 14: 795-804.
    • (1978) Cell , vol.14 , pp. 795-804
    • Hiller, G.1    Weber, K.2
  • 99
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • Himmler A. 1989. Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family. Mol Cell Biol 9: 1389-1396.
    • (1989) Mol Cell Biol , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 100
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated Cterminal microtubule-binding domains and variable Nterminal domains
    • Himmler A, Drechsel D, Kirschner MW, Martin DW Jr. 1989. Tau consists of a set of proteins with repeated Cterminal microtubule-binding domains and variable Nterminal domains. Mol Cell Biol 9: 1381-1388.
    • (1989) Mol Cell Biol , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 101
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa N, Shiomura Y, Okabe S. 1988. Tau proteins: The molecular structure and mode of binding on microtubules. J Cell Biol 107: 1449-1459.
    • (1988) J Cell Biol , vol.107 , pp. 1449-1459
    • Hirokawa, N.1    Shiomura, Y.2    Okabe, S.3
  • 102
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubuleassociated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • Hirokawa N, Funakoshi T, Sato-Harada R, Kanai Y. 1996. Selective stabilization of tau in axons and microtubuleassociated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J Cell Biol 132: 667-679.
    • (1996) J Cell Biol , vol.132 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 103
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility
    • Hoenger A, Sack S, Thormahlen M, Marx A, Muller J, Gross H, Mandelkow E. 1998. Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility. J Cell Biol 141: 419-430.
    • (1998) J Cell Biol , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormahlen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 105
    • 70449753435 scopus 로고    scopus 로고
    • Control of neuronal polarity and plasticity-A renaissance for microtubules?
    • Hoogenraad CC, Bradke F. 2009. Control of neuronal polarity and plasticity-A renaissance for microtubules?. Trends Cell Biol 19: 669-676.
    • (2009) Trends Cell Biol , vol.19 , pp. 669-676
    • Hoogenraad, C.C.1    Bradke, F.2
  • 109
    • 41149156856 scopus 로고    scopus 로고
    • Alzheimer neurofibrillary degeneration: Significance, etiopathogenesis, therapeutics and prevention
    • Iqbal K, Grundke-Iqbal I. 2008. Alzheimer neurofibrillary degeneration: Significance, etiopathogenesis, therapeutics and prevention. J Cell Mol Med 12: 38-55.
    • (2008) J Cell Mol Med , vol.12 , pp. 38-55
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 110
    • 49149105134 scopus 로고    scopus 로고
    • Cytosolic abnormally hyperphosphorylated tau but not paired helical filaments sequester normal MAPs and inhibit microtubule assembly
    • Iqbal K, Alonso Adel C, Grundke-Iqbal I. 2008. Cytosolic abnormally hyperphosphorylated tau but not paired helical filaments sequester normal MAPs and inhibit microtubule assembly. J Alzheimers Dis 14: 365-370.
    • (2008) J Alzheimers Dis , vol.14 , pp. 365-370
    • Iqbal, K.1    Alonso Adel, C.2    Grundke-Iqbal, I.3
  • 113
    • 68949105821 scopus 로고    scopus 로고
    • Phosphorylated Tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease
    • Ittner LM, Ke YD, Gotz J. 2009. Phosphorylated Tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease. J Biol Chem 284: 20909-20916.
    • (2009) J Biol Chem , vol.284 , pp. 20909-20916
    • Ittner, L.M.1    Ke, Y.D.2    Gotz, J.3
  • 116
    • 0033520474 scopus 로고    scopus 로고
    • α-Synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • Jensen PH, Hager H, Nielsen MS, Hojrup P, Gliemann J, Jakes R. 1999. α-Synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J Biol Chem 274: 25481-25489.
    • (1999) J Biol Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5    Jakes, R.6
  • 119
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T, Friedhoff P, Biernat J, Mandelkow EM, Mandelkow E. 1996. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399: 344-349.
    • (1996) FEBS Lett , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 122
  • 124
    • 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
  • 125
    • 0034695259 scopus 로고    scopus 로고
    • 15 A resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa M, Okada Y, Hirokawa N. 2000. 15 A resolution model of the monomeric kinesin motor, KIF1A. Cell 100: 241-252.
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 126
    • 0036469248 scopus 로고    scopus 로고
    • Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinasewith the cytoskeletal protein tau
    • Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J. 2002. Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinasewith the cytoskeletal protein tau. J Neurosci 22: 698-707.
    • (2002) J Neurosci , vol.22 , pp. 698-707
    • Klein, C.1    Kramer, E.M.2    Cardine, A.M.3    Schraven, B.4    Brandt, R.5    Trotter, J.6
  • 127
    • 34548620157 scopus 로고    scopus 로고
    • Swimming against the tide: Mobility of the microtubule-associated protein tau in neurons
    • Konzack S, Thies E, Marx A, Mandelkow EM, Mandelkow E. 2007. Swimming against the tide: Mobility of the microtubule-associated protein tau in neurons. J Neurosci 27: 9916-9927.
    • (2007) J Neurosci , vol.27 , pp. 9916-9927
    • Konzack, S.1    Thies, E.2    Marx, A.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 128
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I. 1993. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 268: 24374-24384.
    • (1993) J Biol Chem , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 129
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ. 1986. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci 83: 4044-4048.
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 131
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik KS, Orecchio LD, Bakalis S, Neve RL. 1989. Developmentally regulated expression of specific tau sequences. Neuron 2: 1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 132
    • 34548389257 scopus 로고    scopus 로고
    • SUT-1 enables tauinduced neurotoxicity in C. elegans
    • Kraemer BC, Schellenberg GD. 2007. SUT-1 enables tauinduced neurotoxicity in C. elegans. Hum Mol Genet 16: 1959-1971.
    • (2007) Hum Mol Genet , vol.16 , pp. 1959-1971
    • Kraemer, B.C.1    Schellenberg, G.D.2
  • 133
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • Ledesma MD, Bonay P, Colaco C, Avila J. 1994. Analysis of microtubule-associated protein tau glycation in paired helical filaments. J Biol Chem 269: 21614-21619.
    • (1994) J Biol Chem , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4
  • 134
    • 0021357249 scopus 로고
    • Calmodulin binds to both microtubule-associated protein 2 and tau proteins
    • Lee YC, Wolff J. 1984. Calmodulin binds to both microtubule-associated protein 2 and tau proteins. J Biol Chem 259: 1226-1230.
    • (1984) J Biol Chem , vol.259 , pp. 1226-1230
    • Lee, Y.C.1    Wolff, J.2
  • 135
    • 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.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 136
  • 138
    • 84863867694 scopus 로고    scopus 로고
    • Developing therapeutic approaches to Tau, selected kinases, and related neuronal protein targets
    • doi: 10.1101/cshperspect.a006437
    • Lee V, Brunden KR, Hutton M, Trojanowski JQ. 2011. Developing therapeutic approaches to Tau, selected kinases, and related neuronal protein targets. Cold Spring Harb Perspect Med doi: 10.1101/cshperspect.a006437.
    • (2011) Cold Spring Harb Perspect Med
    • Lee, V.1    Brunden, K.R.2    Hutton, M.3    Trojanowski, J.Q.4
  • 140
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • Li X, Lu F, Wang JZ, Gong CX. 2006. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur J Neurosci 23: 2078-2086.
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.Z.3    Gong, C.X.4
  • 145
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes
    • LoPresti P, Szuchet S, Papasozomenos SC, Zinkowski RP, Binder LI. 1995. Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes. Proc Natl Acad Sci 92: 10369-10373.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 146
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimerassociated phosphorylated tau protein
    • Lu PJ, Wulf G, Zhou XZ, Davies P, Lu KP. 1999. The prolyl isomerase Pin1 restores the function of Alzheimerassociated phosphorylated tau protein. Nature 399: 784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 148
    • 2342594045 scopus 로고    scopus 로고
    • Evidence for two distinct binding sites for tau on microtubules
    • Makrides V, Massie MR, Feinstein SC, Lew J. 2004. Evidence for two distinct binding sites for tau on microtubules. Proc Natl Acad Sci 101: 6746-6751.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 6746-6751
    • Makrides, V.1    Massie, M.R.2    Feinstein, S.C.3    Lew, J.4
  • 150
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow EM, Thies E, Trinczek B, Biernat J, Mandelkow E. 2004. MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J Cell Biol 167: 99-110.
    • (2004) J Cell Biol , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 151
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai M, Langen R. 2004. Template-assisted filament growth by parallel stacking of tau. Proc Natl Acad Sci 101: 10278-10283.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 152
    • 33846002029 scopus 로고    scopus 로고
    • Side chain-dependent stacking modulates tau filament structure
    • Margittai M, Langen R. 2006. Side chain-dependent stacking modulates tau filament structure. J Biol Chem 281: 37820-37827.
    • (2006) J Biol Chem , vol.281 , pp. 37820-37827
    • Margittai, M.1    Langen, R.2
  • 153
    • 0027945346 scopus 로고
    • Biopsyderived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo ES, Shin RW, Billingsley ML, Van deVoorde A, O'Connor M, Trojanowski JQ, Lee VM. 1994. Biopsyderived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13: 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    van de Voorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 154
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson MP. 2004. Pathways towards and away from Alzheimer's disease. Nature 430: 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 155
    • 0029588380 scopus 로고
    • Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: Evidence for dynamic interactions of tau with microtubules in vivo
    • Mercken M, Fischer I, Kosik KS, Nixon RA. 1995. Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: Evidence for dynamic interactions of tau with microtubules in vivo. J Neurosci 15: 8259-8267.
    • (1995) J Neurosci , vol.15 , pp. 8259-8267
    • Mercken, M.1    Fischer, I.2    Kosik, K.S.3    Nixon, R.A.4
  • 157
    • 38549129613 scopus 로고    scopus 로고
    • The potential for β-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy
    • Mocanu MM, Nissen A, Eckermann K, Khlistunova I, Biernat J, Drexler D, Petrova O, Schonig K, Bujard H, Mandelkow E, et al. 2008. The potential for β-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J Neurosci 28: 737-748.
    • (2008) J Neurosci , vol.28 , pp. 737-748
    • Mocanu, M.M.1    Nissen, A.2    Eckermann, K.3    Khlistunova, I.4    Biernat, J.5    Drexler, D.6    Petrova, O.7    Schonig, K.8    Bujard, H.9    Mandelkow, E.10
  • 159
    • 0347949620 scopus 로고    scopus 로고
    • Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions
    • Moreno-Herrero F, Perez M, Baro AM, Avila J. 2004. Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions. Biophys J 86: 517-525.
    • (2004) Biophys J , vol.86 , pp. 517-525
    • Moreno-Herrero, F.1    Perez, M.2    Baro, A.M.3    Avila, J.4
  • 160
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y. 1993. Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10: 1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 161
    • 0029943566 scopus 로고    scopus 로고
    • The pool of map kinase associated with microtubules is small but constitutively active
    • Morishima-Kawashima M, Kosik KS. 1996. The pool of map kinase associated with microtubules is small but constitutively active. Mol Biol Cell 7: 893-905.
    • (1996) Mol Biol Cell , vol.7 , pp. 893-905
    • Morishima-Kawashima, M.1    Kosik, K.S.2
  • 162
    • 70350455151 scopus 로고    scopus 로고
    • Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway
    • Morita T, Sobue K. 2009. Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway. J Biol Chem 284: 27734-27745.
    • (2009) J Biol Chem , vol.284 , pp. 27734-27745
    • Morita, T.1    Sobue, K.2
  • 165
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate {β}-structure and bind to microtubules and polyanions
    • Mukrasch MD, Biernat J, von Bergen M, Griesinger C, Mandelkow E, Zweckstetter M. 2005. Sites of tau important for aggregation populate {β}-structure and bind to microtubules and polyanions. J Biol Chem 280: 24978-24986.
    • (2005) J Biol Chem , vol.280 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 169
    • 0141656303 scopus 로고    scopus 로고
    • Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head
    • Nakata T, Hirokawa N. 2003. Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head. J Cell Biol 162: 1045-1055.
    • (2003) J Cell Biol , vol.162 , pp. 1045-1055
    • Nakata, T.1    Hirokawa, N.2
  • 170
    • 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
    • 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 the genes for tau and microtubule-associated protein 2. Brain Res 387: 271-280.
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 172
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB. 1990. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature 347: 256-261.
    • (1990) Nature , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 173
    • 4043167747 scopus 로고    scopus 로고
    • Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM. 2004. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43: 321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 174
    • 0025161635 scopus 로고
    • Calmodulin binds to a tubulin binding site of the microtubule-associated protein tau
    • Padilla R, Maccioni RB, Avila J. 1990. Calmodulin binds to a tubulin binding site of the microtubule-associated protein tau. Mol Cell Biochem 97: 35-41.
    • (1990) Mol Cell Biochem , vol.97 , pp. 35-41
    • Padilla, R.1    Maccioni, R.B.2    Avila, J.3
  • 175
    • 0042924434 scopus 로고    scopus 로고
    • Differential regulation of microtubule dynamics by three-and four-repeat tau: Implications for the onset of neurodegenerative disease
    • Panda D, Samuel JC, Massie M, Feinstein SC, Wilson L. 2003. Differential regulation of microtubule dynamics by three-and four-repeat tau: Implications for the onset of neurodegenerative disease. Proc Natl Acad Sci 100: 9548-9553.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 176
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of Tau in the central nervous system
    • Papasozomenos SC, Binder LI. 1987. Phosphorylation determines two distinct species of Tau in the central nervous system. Cell Motil Cytoskeleton 8: 210-226.
    • (1987) Cell Motil Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 177
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates β-amyloid-induced neurodegeneration
    • Park SY, Ferreira A. 2005. The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates β-amyloid-induced neurodegeneration. J Neurosci 25: 5365-5375.
    • (2005) J Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 178
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Perez M, Valpuesta JM, Medina M, Montejo de Garcini E, Avila J. 1996. Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction. J Neurochem 67: 1183-1190.
    • (1996) J Neurochem , vol.67 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo de Garcini, E.4    Avila, J.5
  • 184
    • 0030635801 scopus 로고    scopus 로고
    • Paired helical filaments are twisted ribbons composed of two parallel and aligned components: Image reconstruction and modeling of filament structure using atomic force microscopy
    • Pollanen MS, Markiewicz P, Goh MC. 1997. Paired helical filaments are twisted ribbons composed of two parallel and aligned components: Image reconstruction and modeling of filament structure using atomic force microscopy. J Neuropathol Exp Neurol 56: 79-85.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 79-85
    • Pollanen, M.S.1    Markiewicz, P.2    Goh, M.C.3
  • 186
    • 34250854596 scopus 로고    scopus 로고
    • Nitration in neurodegeneration: Deciphering the "Hows" "nYs"
    • Reynolds MR, Berry RW, Binder LI. 2007. Nitration in neurodegeneration: Deciphering the "Hows" "nYs". Biochemistry 46: 7325-7336.
    • (2007) Biochemistry , vol.46 , pp. 7325-7336
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 187
    • 49649119504 scopus 로고    scopus 로고
    • Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cg1, Grb2, and Src family kinases
    • Reynolds CH, Garwood CJ, Wray S, Price C, Kellie S, Perera T, Zvelebil M, Yang A, Sheppard PW, Varndell IM, et al. 2008. Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cg1, Grb2, and Src family kinases. J Biol Chem 283: 18177-18186.
    • (2008) J Biol Chem , vol.283 , pp. 18177-18186
    • Reynolds, C.H.1    Garwood, C.J.2    Wray, S.3    Price, C.4    Kellie, S.5    Perera, T.6    Zvelebil, M.7    Yang, A.8    Sheppard, P.W.9    Varndell, I.M.10
  • 190
    • 1842432582 scopus 로고    scopus 로고
    • MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain
    • Roger B, Al-Bassam J, Dehmelt L, Milligan RA, Halpain S. 2004. MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr Biol 14: 363-371.
    • (2004) Curr Biol , vol.14 , pp. 363-371
    • Roger, B.1    Al-Bassam, J.2    Dehmelt, L.3    Milligan, R.A.4    Halpain, S.5
  • 192
    • 78649767505 scopus 로고    scopus 로고
    • Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease
    • Salminen A, Ojala J, Kaarniranta K, Hiltunen M, Soininen H. 2011. Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease. Prog Neurobiol 93: 99-110.
    • (2011) Prog Neurobiol , vol.93 , pp. 99-110
    • Salminen, A.1    Ojala, J.2    Kaarniranta, K.3    Hiltunen, M.4    Soininen, H.5
  • 196
    • 57049139853 scopus 로고    scopus 로고
    • Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone
    • Sarkar M, Kuret J, Lee G. 2008. Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone. J Neurosci Res 86: 2763-2773.
    • (2008) J Neurosci Res , vol.86 , pp. 2763-2773
    • Sarkar, M.1    Kuret, J.2    Lee, G.3
  • 198
    • 34249008806 scopus 로고    scopus 로고
    • Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
    • Schaap IA, Hoffmann B, Carrasco C, Merkel R, Schmidt CF. 2007. Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules. J Struct Biol 158: 282-292.
    • (2007) J Struct Biol , vol.158 , pp. 282-292
    • Schaap, I.A.1    Hoffmann, B.2    Carrasco, C.3    Merkel, R.4    Schmidt, C.F.5
  • 199
    • 46749113005 scopus 로고    scopus 로고
    • Tau-based treatment strategies in neurodegenerative diseases
    • Schneider A, Mandelkow E. 2008. Tau-based treatment strategies in neurodegenerative diseases. Neurotherapeutics 5: 443-457.
    • (2008) Neurotherapeutics , vol.5 , pp. 443-457
    • Schneider, A.1    Mandelkow, E.2
  • 200
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A, Biernat J, von Bergen M, Mandelkow E, Mandelkow EM. 1999. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38: 3549-3558.
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 201
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure
    • SchweersO, Schonbrunn-Hanebeck E, Marx A, Mandelkow E. 1994. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure. J Biol Chem 269: 24290-24297.
    • (1994) J Biol Chem , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 202
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • SchweersO, Mandelkow EM, Biernat J, Mandelkow E. 1995. Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc Natl Acad Sci 92: 8463-8467.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 203
    • 35348936103 scopus 로고    scopus 로고
    • Beyond amyloid: The next generation of Alzheimer's disease therapeutics
    • Seabrook GR, Ray WJ, Shearman M, Hutton M. 2007. Beyond amyloid: The next generation of Alzheimer's disease therapeutics. Mol Interv 7: 261-270.
    • (2007) Mol Interv , vol.7 , pp. 261-270
    • Seabrook, G.R.1    Ray, W.J.2    Shearman, M.3    Hutton, M.4
  • 204
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A, Kojima H, Oiwa K, Mandelkow EM, Song YH, Mandelkow E. 2002. Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J 21: 4896-4905.
    • (2002) EMBO J , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 207
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptordependent signaling pathway
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL. 2007. Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptordependent signaling pathway. J Neurosci 27: 2866-2875.
    • (2007) J Neurosci , vol.27 , 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
  • 208
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Shimura H, Miura-Shimura Y, Kosik KS. 2004a. Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J Biol Chem 279: 17957-17962.
    • (2004) J Biol Chem , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 209
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H, Schwartz D, Gygi SP, Kosik KS. 2004b. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem 279: 4869-4876.
    • (2004) J Biol Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 213
    • 69249212121 scopus 로고    scopus 로고
    • Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3z
    • Sluchanko NN, Seit-Nebi AS, Gusev NB. 2009. Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3z. FEBS Lett 583: 2739-2742.
    • (2009) FEBS Lett , vol.583 , pp. 2739-2742
    • Sluchanko, N.N.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 215
    • 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 3rd, 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.
    • (1999) J Biol Chem , vol.274 , 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
  • 218
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM. 2002. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 156: 1051-1063.
    • (2002) J Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 219
    • 0025013270 scopus 로고
    • Phosphorylation of microtubule-associated protein tau: Identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles
    • Steiner B, Mandelkow EM, Biernat J, Gustke N, Meyer HE, Schmidt B, Mieskes G, Soling HD, Drechsel D, Kirschner MW, et al. 1990. Phosphorylation of microtubule-associated protein tau: Identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles. EMBO J 9: 3539-3544.
    • (1990) EMBO J , vol.9 , pp. 3539-3544
    • Steiner, B.1    Mandelkow, E.M.2    Biernat, J.3    Gustke, N.4    Meyer, H.E.5    Schmidt, B.6    Mieskes, G.7    Soling, H.D.8    Drechsel, D.9    Kirschner, M.W.10
  • 220
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff WH, Johnson GV. 2005. Tau phosphorylation: Physiological and pathological consequences. Biochim Biophys Acta 1739: 280-297.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 224
    • 79951818085 scopus 로고    scopus 로고
    • Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant
    • Sydow A, Van der Jeugd A, Zheng F, Ahmed T, Balschun D, Petrova O, Drexler D, Zhou L, Rune G, Mandelkow E, et al. 2011. Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant. J Neurosci 31: 2511-2525.
    • (2011) J Neurosci , vol.31 , pp. 2511-2525
    • Sydow, A.1    van der Jeugd, A.2    Zheng, F.3    Ahmed, T.4    Balschun, D.5    Petrova, O.6    Drexler, D.7    Zhou, L.8    Rune, G.9    Mandelkow, E.10
  • 226
    • 19544362550 scopus 로고    scopus 로고
    • Upregulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H, Grundke-Iqbal I, Iqbal K. 2005. Upregulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am J Pathol 166: 1761-1771.
    • (2005) Am J Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 227
    • 0036047004 scopus 로고    scopus 로고
    • Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
    • Terwel D, Dewachter I, Van Leuven F. 2002. Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease. Neuromolecular Med 2: 151-165.
    • (2002) Neuromolecular Med , vol.2 , pp. 151-165
    • Terwel, D.1    Dewachter, I.2    van Leuven, F.3
  • 228
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies E, MandelkowEM. 2007. Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J Neurosci 27: 2896-2907.
    • (2007) J Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 229
    • 67849111948 scopus 로고    scopus 로고
    • Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein
    • Tortosa E, Santa-Maria I, Moreno F, Lim F, Perez M, Avila J. 2009. Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. JAlzheimers Dis 17: 319-325.
    • (2009) JAlzheimers Dis , vol.17 , pp. 319-325
    • Tortosa, E.1    Santa-Maria, I.2    Moreno, F.3    Lim, F.4    Perez, M.5    Avila, J.6
  • 230
    • 0027446346 scopus 로고
    • Dynamics of microtubules bundled by microtubule associated protein 2C (MAP2C)
    • Umeyama T, Okabe S, Kanai Y, Hirokawa N. 1993. Dynamics of microtubules bundled by microtubule associated protein 2C (MAP2C). J Cell Biol 120: 451-465.
    • (1993) J Cell Biol , vol.120 , pp. 451-465
    • Umeyama, T.1    Okabe, S.2    Kanai, Y.3    Hirokawa, N.4
  • 231
    • 27844470590 scopus 로고    scopus 로고
    • Molecular motors implicated in the axonal transport of tau and α-synuclein
    • Utton MA, Noble WJ, Hill JE, Anderton BH, Hanger DP. 2005. Molecular motors implicated in the axonal transport of tau and α-synuclein. J Cell Sci 118: 4645-4654.
    • (2005) J Cell Sci , vol.118 , pp. 4645-4654
    • Utton, M.A.1    Noble, W.J.2    Hill, J.E.3    Anderton, B.H.4    Hanger, D.P.5
  • 233
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306)VQIVYK(311) forming β structure
    • von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E. 2000. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306)VQIVYK(311) forming β structure. Proc Natl Acad Sci 97: 5129-5134.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 5129-5134
    • von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 234
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure
    • von Bergen M, Barghorn S, Li L, Marx A, Biernat J, MandelkowEM, MandelkowE. 2001. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure. J Biol Chem 276: 48165-48174.
    • (2001) J Biol Chem , vol.276 , pp. 48165-48174
    • von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 236
    • 4544300178 scopus 로고    scopus 로고
    • Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo
    • Watanabe A, Hong WK, Dohmae N, Takio K, Morishima-Kawashima M, Ihara Y. 2004. Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. J Neurochem 90: 1302-1311.
    • (2004) J Neurochem , vol.90 , pp. 1302-1311
    • Watanabe, A.1    Hong, W.K.2    Dohmae, N.3    Takio, K.4    Morishima-Kawashima, M.5    Ihara, Y.6
  • 237
    • 77956242962 scopus 로고    scopus 로고
    • Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability
    • Wegmann S, Jung YJ, Chinnathambi S, Mandelkow EM, Mandelkow E, Muller DJ. 2010. Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability. J Biol Chem 285: 27302-27313.
    • (2010) J Biol Chem , vol.285 , pp. 27302-27313
    • Wegmann, S.1    Jung, Y.J.2    Chinnathambi, S.3    Mandelkow, E.M.4    Mandelkow, E.5    Muller, D.J.6
  • 239
    • 0015520152 scopus 로고
    • Microtubule formation in vitro in solutions containing low calcium concentrations
    • Weisenberg RC. 1972. Microtubule formation in vitro in solutions containing low calcium concentrations. Science 177: 1104-1105.
    • (1972) Science , vol.177 , pp. 1104-1105
    • Weisenberg, R.C.1
  • 241
  • 242
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H, Drewes G, Biernat J, Mandelkow EM, Mandelkow E. 1992. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 118: 573-584.
    • (1992) J Cell Biol , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 243
    • 43249114144 scopus 로고    scopus 로고
    • Membrane-bound β-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism
    • Williamson R, Usardi A, Hanger DP, Anderton BH. 2008. Membrane-bound β-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism. FASEB J 22: 1552-1559.
    • (2008) FASEB J , vol.22 , pp. 1552-1559
    • Williamson, R.1    Usardi, A.2    Hanger, D.P.3    Anderton, B.H.4
  • 244
    • 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
  • 245
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson DM, Binder LI. 1997. Free fatty acids stimulate the polymerization of tau and amyloid β peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am J Pathol 150: 2181-2195.
    • (1997) Am J Pathol , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 246
    • 11244309692 scopus 로고    scopus 로고
    • New microtubule/tubulintargeted anticancer drugs and novel chemotherapeutic strategies
    • Wilson L, Jordan MA. 2004. New microtubule/tubulintargeted anticancer drugs and novel chemotherapeutic strategies. J Chemother 16: 83-85.
    • (2004) J Chemother , vol.16 , pp. 83-85
    • Wilson, L.1    Jordan, M.A.2
  • 248
    • 65249116483 scopus 로고    scopus 로고
    • Tau mutations in neurodegenerative diseases
    • Wolfe MS. 2009. Tau mutations in neurodegenerative diseases. J Biol Chem 284: 6021-6025.
    • (2009) J Biol Chem , vol.284 , pp. 6021-6025
    • Wolfe, M.S.1
  • 249
    • 0022457104 scopus 로고
    • A neuronal antigen in the brains of Alzheimer patients
    • Wolozin BL, Pruchnicki A, Dickson DW, Davies P. 1986. A neuronal antigen in the brains of Alzheimer patients. Science 232: 648-650.
    • (1986) Science , vol.232 , pp. 648-650
    • Wolozin, B.L.1    Pruchnicki, A.2    Dickson, D.W.3    Davies, P.4
  • 250
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)
    • Wood JG, Mirra SS, Pollock NJ, Binder LI. 1986. Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc Natl Acad Sci 83: 4040-4043.
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3    Binder, L.I.4
  • 252
    • 77956587739 scopus 로고    scopus 로고
    • Aβ oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • Zempel H, Thies E, Mandelkow E, Mandelkow EM. 2010. Aβ oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J Neurosci 30: 11938-11950.
    • (2010) J Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.