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Volumn 52, Issue 24, 2013, Pages 4107-4126

Mechanistic studies unravel the complexity inherent in tau aggregation leading to Alzheimer's disease and the tauopathies

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; BIOPHYSICAL STUDIES; COGNITIVE DECLINE; DISEASE PROGRESSION; MECHANISTIC STUDIES; NEURODEGENERATION; NEURODEGENERATIVE; STRUCTURE FUNCTIONS;

EID: 84879237541     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400209z     Document Type: Article
Times cited : (46)

References (212)
  • 2
    • 0034826896 scopus 로고    scopus 로고
    • Regulation of microtubule-associated proteins
    • Cassimeris, L. and Spittle, C. (2001) Regulation of microtubule- associated proteins Int. Rev. Cytol. 210, 163-226
    • (2001) Int. Rev. Cytol. , vol.210 , pp. 163-226
    • Cassimeris, L.1    Spittle, C.2
  • 3
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland, D. W., Hwo, S. Y., and Kirschner, M. W. (1977) 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
  • 4
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland, D. W., Hwo, S. Y., and Kirschner, M. W. (1977) 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
  • 5
    • 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, R. L., Harris, P., Kosik, K. S., Kurnit, D. M., and Donlon, T. A. (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
  • 6
    • 0026488111 scopus 로고
    • Structure and novel exons of the human tau gene
    • Andreadis, A., Brown, W. M., and Kosik, K. S. (1992) Structure and novel exons of the human tau gene Biochemistry 31, 10626-10633
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 7
    • 0029843684 scopus 로고    scopus 로고
    • Tau is widely expressed in rat tissues
    • Gu, Y., Oyama, F., and 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
  • 8
    • 0024529404 scopus 로고
    • Distribution of tau proteins in the normal human central and peripheral nervous system
    • Trojanowski, J. Q., Schuck, T., Schmidt, M. L., and Lee, V. M. (1989) Distribution of tau proteins in the normal human central and peripheral nervous system J. Histochem. Cytochem. 37, 209-215
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 209-215
    • Trojanowski, J.Q.1    Schuck, T.2    Schmidt, M.L.3    Lee, V.M.4
  • 9
    • 0023911326 scopus 로고
    • Light and electron microscope localization of the microtubule-associated tau protein in rat brain
    • Migheli, A., Butler, M., Brown, K., and Shelanski, M. L. (1988) Light and electron microscope localization of the microtubule-associated tau protein in rat brain J. Neurosci. 8, 1846-1851
    • (1988) J. Neurosci. , vol.8 , pp. 1846-1851
    • Migheli, A.1    Butler, M.2    Brown, K.3    Shelanski, M.L.4
  • 11
    • 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, C. M., Crowther, R. A., Walker, J. E., and 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. U.S.A. 85, 4051-4055
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 12
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee, G., Cowan, N., and 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
  • 13
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A., Drechsel, D., Kirschner, M. W., and Martin, D. W., Jr. (1989) Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal 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
  • 14
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert, M. and Jakes, R. (1990) Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization EMBO J. 9, 4225-4230
    • (1990) EMBO J. , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 17
    • 0017600295 scopus 로고
    • Removal of the projections from cytoplasmic microtubules in vitro by digestion with trypsin
    • Vallee, R. B. and Borisy, G. G. (1977) Removal of the projections from cytoplasmic microtubules in vitro by digestion with trypsin J. Biol. Chem. 252, 377-382
    • (1977) J. Biol. Chem. , vol.252 , pp. 377-382
    • Vallee, R.B.1    Borisy, G.G.2
  • 18
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa, N., Shiomura, Y., and 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
  • 19
    • 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, M. G., Potier, M. C., Ulrich, J., and Crowther, R. A. (1989) 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
    • (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
  • 21
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure
    • Schweers, O., Schonbrunn-Hanebeck, E., Marx, A., and 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
  • 22
    • 52949123661 scopus 로고    scopus 로고
    • Domain conformation of tau protein studied by solution small-angle X-ray scattering
    • Mylonas, E., Hascher, A., Bernado, P., Blackledge, M., Mandelkow, E., and Svergun, D. I. (2008) Domain conformation of tau protein studied by solution small-angle X-ray scattering Biochemistry 47, 10345-10353
    • (2008) Biochemistry , vol.47 , pp. 10345-10353
    • Mylonas, E.1    Hascher, A.2    Bernado, P.3    Blackledge, M.4    Mandelkow, E.5    Svergun, D.I.6
  • 23
    • 4344704080 scopus 로고    scopus 로고
    • Reassessing random-coil statistics in unfolded proteins
    • Fitzkee, N. C. and Rose, G. D. (2004) Reassessing random-coil statistics in unfolded proteins Proc. Natl. Acad. Sci. U.S.A. 101, 12497-12502
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12497-12502
    • Fitzkee, N.C.1    Rose, G.D.2
  • 24
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha, G. A., Bowser, R., Kazam, I. G., and Davies, P. (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau J. Neurosci. Res. 48, 128-132
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 25
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel, G., Mager, E. M., Binder, L. I., and Kuret, J. (1996) The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology J. Biol. Chem. 271, 32789-32795
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 27
    • 84867390250 scopus 로고    scopus 로고
    • Identification of an aggregation-prone structure of tau
    • Elbaum-Garfinkle, S. and Rhoades, E. (2012) Identification of an aggregation-prone structure of tau J. Am. Chem. Soc. 134, 16607-16613
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16607-16613
    • Elbaum-Garfinkle, S.1    Rhoades, E.2
  • 28
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode, B. L. and Feinstein, S. C. (1994) Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau J. Cell Biol. 124, 769-782
    • (1994) J. Cell Biol. , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 29
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K. A. and Kirschner, M. W. (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
    • 84871199132 scopus 로고    scopus 로고
    • Taxol-stabilized microtubules promote the formation of filaments from unmodified full-length tau in vitro
    • Duan, A. R. and Goodson, H. V. (2012) Taxol-stabilized microtubules promote the formation of filaments from unmodified full-length tau in vitro Mol. Biol. Cell 23, 4796-4806
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4796-4806
    • Duan, A.R.1    Goodson, H.V.2
  • 32
    • 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., and 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
  • 33
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • Goode, B. L., Denis, P. E., Panda, D., Radeke, M. J., Miller, H. P., Wilson, L., and Feinstein, S. C. (1997) Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly Mol. Biol. Cell 8, 353-365
    • (1997) Mol. Biol. Cell , vol.8 , pp. 353-365
    • Goode, B.L.1    Denis, P.E.2    Panda, D.3    Radeke, M.J.4    Miller, H.P.5    Wilson, L.6    Feinstein, S.C.7
  • 35
    • 0033607298 scopus 로고    scopus 로고
    • Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau
    • Panda, D., Miller, H. P., and Wilson, L. (1999) Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau Proc. Natl. Acad. Sci. U.S.A. 96, 12459-12464
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12459-12464
    • Panda, D.1    Miller, H.P.2    Wilson, L.3
  • 36
    • 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, J. C., Massie, M., Feinstein, S. C., and 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. U.S.A. 100, 9548-9553
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 37
    • 0032147118 scopus 로고    scopus 로고
    • Functional protein domains from the thermally driven motion of polypeptide chains: A proposal
    • Hoh, J. H. (1998) Functional protein domains from the thermally driven motion of polypeptide chains: A proposal Proteins 32, 223-228
    • (1998) Proteins , vol.32 , pp. 223-228
    • Hoh, J.H.1
  • 38
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow, E. M. and Mandelkow, E. (2012) Biochemistry and cell biology of tau protein in neurofibrillary degeneration Cold Spring Harbor Perspect. Med. 2, a006247
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 006247
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 39
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen, J., Kanai, Y., Cowan, N. J., and 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
  • 40
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit, R., Ross, J. L., Goldman, Y. E., and Holzbaur, E. L. (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
  • 43
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt, R., Leger, J., and Lee, G. (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain J. Cell Biol. 131, 1327-1340
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 45
    • 70350435136 scopus 로고    scopus 로고
    • Activated actin-depolymerizing factor/cofilin sequesters phosphorylated microtubule-associated protein during the assembly of Alzheimer-like neuritic cytoskeletal striations
    • Whiteman, I. T., Gervasio, O. L., Cullen, K. M., Guillemin, G. J., Jeong, E. V., Witting, P. K., Antao, S. T., Minamide, L. S., Bamburg, J. R., and Goldsbury, C. (2009) Activated actin-depolymerizing factor/cofilin sequesters phosphorylated microtubule-associated protein during the assembly of Alzheimer-like neuritic cytoskeletal striations J. Neurosci. 29, 12994-13005
    • (2009) J. Neurosci. , vol.29 , pp. 12994-13005
    • Whiteman, I.T.1    Gervasio, O.L.2    Cullen, K.M.3    Guillemin, G.J.4    Jeong, E.V.5    Witting, P.K.6    Antao, S.T.7    Minamide, L.S.8    Bamburg, J.R.9    Goldsbury, C.10
  • 47
    • 77953524779 scopus 로고    scopus 로고
    • Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding
    • Leugers, C. J. and Lee, G. (2010) Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding J. Biol. Chem. 285, 19125-19134
    • (2010) J. Biol. Chem. , vol.285 , pp. 19125-19134
    • Leugers, C.J.1    Lee, G.2
  • 51
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura, H., Schwartz, D., Gygi, S. P., and Kosik, K. S. (2004) 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
  • 52
    • 0032211045 scopus 로고    scopus 로고
    • Acute inactivation of tau has no effect on dynamics of microtubules in growing axons of cultured sympathetic neurons
    • Tint, I., Slaughter, T., Fischer, I., and Black, M. M. (1998) Acute inactivation of tau has no effect on dynamics of microtubules in growing axons of cultured sympathetic neurons J. Neurosci. 18, 8660-8673
    • (1998) J. Neurosci. , vol.18 , pp. 8660-8673
    • Tint, I.1    Slaughter, T.2    Fischer, I.3    Black, M.M.4
  • 54
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., and Vitek, M. P. (2001) Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice J. Cell Sci. 114, 1179-1187
    • (2001) J. Cell Sci. , vol.114 , pp. 1179-1187
    • Dawson, H.N.1    Ferreira, A.2    Eyster, M.V.3    Ghoshal, N.4    Binder, L.I.5    Vitek, M.P.6
  • 55
    • 0035152814 scopus 로고    scopus 로고
    • Neurotrophins are required for nerve growth during development
    • Tucker, K. L., Meyer, M., and Barde, Y. A. (2001) Neurotrophins are required for nerve growth during development Nat. Neurosci. 4, 29-37
    • (2001) Nat. Neurosci. , vol.4 , pp. 29-37
    • Tucker, K.L.1    Meyer, M.2    Barde, Y.A.3
  • 57
  • 58
    • 39549117998 scopus 로고    scopus 로고
    • Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice
    • Yuan, A., Kumar, A., Peterhoff, C., Duff, K., and Nixon, R. A. (2008) Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice J. Neurosci. 28, 1682-1687
    • (2008) J. Neurosci. , vol.28 , pp. 1682-1687
    • Yuan, A.1    Kumar, A.2    Peterhoff, C.3    Duff, K.4    Nixon, R.A.5
  • 59
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami, S., Harada, A., and Hirokawa, N. (2000) Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice Neurosci. Lett. 279, 129-132
    • (2000) Neurosci. Lett. , vol.279 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 60
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-β and tau: A toxic pas de deux in Alzheimer's disease
    • Ittner, L. M. and Gotz, J. (2011) Amyloid-β and tau: A toxic pas de deux in Alzheimer's disease Nat. Rev. Neurosci. 12, 65-72
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 61
    • 0034605045 scopus 로고    scopus 로고
    • Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
    • Takei, Y., Teng, J., Harada, A., and Hirokawa, N. (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes J. Cell Biol. 150, 989-1000
    • (2000) J. Cell Biol. , vol.150 , pp. 989-1000
    • Takei, Y.1    Teng, J.2    Harada, A.3    Hirokawa, N.4
  • 62
    • 0035140975 scopus 로고    scopus 로고
    • Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease
    • Garcia, M. L. and Cleveland, D. W. (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
  • 64
  • 66
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., and Hyman, B. T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease Neurology 42, 631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 67
    • 0019935804 scopus 로고
    • Plaques, tangles and dementia. A quantitative study
    • Wilcock, G. K. and Esiri, M. M. (1982) Plaques, tangles and dementia. A quantitative study J. Neurol. Sci. 56, 343-356
    • (1982) J. Neurol. Sci. , vol.56 , pp. 343-356
    • Wilcock, G.K.1    Esiri, M.M.2
  • 71
    • 26444581827 scopus 로고    scopus 로고
    • Tau gene mutations and their effects
    • Goedert, M. (2005) Tau gene mutations and their effects Mov. Disord. 20 (Suppl. 12) S45-S52
    • (2005) Mov. Disord. , vol.20 , Issue.SUPPL. 12
    • Goedert, M.1
  • 72
    • 0032561415 scopus 로고    scopus 로고
    • Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly
    • Hasegawa, M., Smith, M. J., and Goedert, M. (1998) Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly FEBS Lett. 437, 207-210
    • (1998) FEBS Lett. , vol.437 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 74
    • 84862027756 scopus 로고    scopus 로고
    • Tau isoform composition influences rate and extent of filament formation
    • Zhong, Q., Congdon, E. E., Nagaraja, H. N., and Kuret, J. (2012) Tau isoform composition influences rate and extent of filament formation J. Biol. Chem. 287, 20711-20719
    • (2012) J. Biol. Chem. , vol.287 , pp. 20711-20719
    • Zhong, Q.1    Congdon, E.E.2    Nagaraja, H.N.3    Kuret, J.4
  • 75
    • 33748995351 scopus 로고    scopus 로고
    • Untangling the tau gene association with neurodegenerative disorders
    • Pittman, A. M., Fung, H. C., and de Silva, R. (2006) Untangling the tau gene association with neurodegenerative disorders Hum. Mol. Genet. 15 (Spec. No. 2) R188-R195
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.SPEC. NO. 2
    • Pittman, A.M.1    Fung, H.C.2    De Silva, R.3
  • 77
    • 4143134235 scopus 로고    scopus 로고
    • The future of association studies: Gene-based analysis and replication
    • Neale, B. M. and Sham, P. C. (2004) The future of association studies: Gene-based analysis and replication Am. J. Hum. Genet. 75, 353-362
    • (2004) Am. J. Hum. Genet. , vol.75 , pp. 353-362
    • Neale, B.M.1    Sham, P.C.2
  • 78
    • 84864390773 scopus 로고    scopus 로고
    • Tau alternative splicing in familial and sporadic tauopathies
    • Niblock, M. and Gallo, J. M. (2012) Tau alternative splicing in familial and sporadic tauopathies Biochem. Soc. Trans. 40, 677-680
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 677-680
    • Niblock, M.1    Gallo, J.M.2
  • 81
    • 0042125603 scopus 로고    scopus 로고
    • Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals
    • Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rudiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., and Hartig, W. (2003) Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals J. Neurosci. 23, 6972-6981
    • (2003) J. Neurosci. , vol.23 , pp. 6972-6981
    • Arendt, T.1    Stieler, J.2    Strijkstra, A.M.3    Hut, R.A.4    Rudiger, J.5    Van Der Zee, E.A.6    Harkany, T.7    Holzer, M.8    Hartig, W.9
  • 83
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L., and Selkoe, D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease Proc. Natl. Acad. Sci. U.S.A. 83, 4044-4048
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 84
    • 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
  • 85
    • 0025977281 scopus 로고
    • Straight and paired helical filaments in Alzheimer disease have a common structural unit
    • Crowther, R. A. (1991) Straight and paired helical filaments in Alzheimer disease have a common structural unit Proc. Natl. Acad. Sci. U.S.A. 88, 2288-2292
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2288-2292
    • Crowther, R.A.1
  • 86
    • 0028223431 scopus 로고
    • Twisted ribbon structure of paired helical filaments revealed by atomic force m icroscopy
    • Pollanen, M. S., Markiewicz, P., Bergeron, C., and Goh, M. C. (1994) Twisted ribbon structure of paired helical filaments revealed by atomic force m icroscopy Am. J. Pathol. 144, 869-873
    • (1994) Am. J. Pathol. , vol.144 , pp. 869-873
    • Pollanen, M.S.1    Markiewicz, P.2    Bergeron, C.3    Goh, M.C.4
  • 87
    • 0347949620 scopus 로고    scopus 로고
    • Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions
    • Moreno-Herrero, F., Perez, M., Baro, A. M., and 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
  • 88
    • 77956242962 scopus 로고    scopus 로고
    • Human tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability
    • Wegmann, S., Jung, Y. J., Chinnathambi, S., Mandelkow, E. M., Mandelkow, E., and Muller, D. J. (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
  • 90
    • 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, E. M., and 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. U.S.A. 97, 5129-5134
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 91
    • 0036830506 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
    • Li, L., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2002) Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis J. Biol. Chem. 277, 41390-41400
    • (2002) J. Biol. Chem. , vol.277 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 92
    • 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, L. C., Oberg, K. A., Fink, A. L., Goedert, M., and Crowther, R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure Proc. Natl. Acad. Sci. U.S.A. 100, 9034-9038
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 93
    • 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., Mandelkow, E. M., and Mandelkow, E. (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
  • 95
    • 46649101161 scopus 로고    scopus 로고
    • Nucleation-dependent tau filament formation: The importance of dimerization and an estimation of elementary rate constants
    • Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Matzavinos, A., and Kuret, J. (2008) Nucleation-dependent tau filament formation: The importance of dimerization and an estimation of elementary rate constants J. Biol. Chem. 283, 13806-13816
    • (2008) J. Biol. Chem. , vol.283 , pp. 13806-13816
    • Congdon, E.E.1    Kim, S.2    Bonchak, J.3    Songrug, T.4    Matzavinos, A.5    Kuret, J.6
  • 96
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai, M. and Langen, R. (2004) Template-assisted filament growth by parallel stacking of tau Proc. Natl. Acad. Sci. U.S.A. 101, 10278-10283
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 97
    • 33846002029 scopus 로고    scopus 로고
    • Side chain-dependent stacking modulates tau filament structure
    • Margittai, M. and 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
  • 98
    • 42949135930 scopus 로고    scopus 로고
    • Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy
    • Andronesi, O. C., von Bergen, M., Biernat, J., Seidel, K., Griesinger, C., Mandelkow, E., and Baldus, M. (2008) Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy J. Am. Chem. Soc. 130, 5922-5928
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5922-5928
    • Andronesi, O.C.1    Von Bergen, M.2    Biernat, J.3    Seidel, K.4    Griesinger, C.5    Mandelkow, E.6    Baldus, M.7
  • 100
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments
    • Jeganathan, S., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2008) The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments Biochemistry 47, 10526-10539
    • (2008) Biochemistry , vol.47 , pp. 10526-10539
    • Jeganathan, S.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 101
    • 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, M. M., Nissen, A., Eckermann, K., Khlistunova, I., Biernat, J., Drexler, D., Petrova, O., Schonig, K., Bujard, H., Mandelkow, E., Zhou, L., Rune, G., and Mandelkow, E. M. (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    Zhou, L.11    Rune, G.12    Mandelkow, E.M.13
  • 103
    • 33646155955 scopus 로고    scopus 로고
    • Structure of core domain of fibril-forming PHF/tau fragments
    • Inouye, H., Sharma, D., Goux, W. J., and Kirschner, D. A. (2006) Structure of core domain of fibril-forming PHF/tau fragments Biophys. J. 90, 1774-1789
    • (2006) Biophys. J. , vol.90 , pp. 1774-1789
    • Inouye, H.1    Sharma, D.2    Goux, W.J.3    Kirschner, D.A.4
  • 107
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D. and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66, 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 108
    • 35648945914 scopus 로고    scopus 로고
    • Protein aggregation processes: In search of the mechanism
    • Frieden, C. (2007) Protein aggregation processes: In search of the mechanism Protein Sci. 16, 2334-2344
    • (2007) Protein Sci. , vol.16 , pp. 2334-2344
    • Frieden, C.1
  • 109
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris, A. M., Watzky, M. A., and Finke, R. G. (2009) Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature Biochim. Biophys. Acta 1794, 375-397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 110
    • 67649366306 scopus 로고    scopus 로고
    • Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies
    • Bernacki, J. P. and Murphy, R. M. (2009) Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies Biophys. J. 96, 2871-2887
    • (2009) Biophys. J. , vol.96 , pp. 2871-2887
    • Bernacki, J.P.1    Murphy, R.M.2
  • 111
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone, F. (1999) Analysis of protein aggregation kinetics Methods Enzymol. 309, 256-274
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 112
    • 0019474894 scopus 로고
    • The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers
    • Erickson, H. P. and Pantaloni, D. (1981) The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers Biophys. J. 34, 293-309
    • (1981) Biophys. J. , vol.34 , pp. 293-309
    • Erickson, H.P.1    Pantaloni, D.2
  • 113
    • 0021527508 scopus 로고
    • Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway
    • Bishop, M. F. and Ferrone, F. A. (1984) Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway Biophys. J. 46, 631-644
    • (1984) Biophys. J. , vol.46 , pp. 631-644
    • Bishop, M.F.1    Ferrone, F.A.2
  • 114
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts, C. J. (2007) Non-native protein aggregation kinetics Biotechnol. Bioeng. 98, 927-938
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 115
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • Oosawa, F. and Kasai, M. (1962) A theory of linear and helical aggregations of macromolecules J. Mol. Biol. 4, 10-21
    • (1962) J. Mol. Biol. , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 116
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of amyloid β-protein for structural and functional studies
    • Teplow, D. B. (2006) Preparation of amyloid β-protein for structural and functional studies Methods Enzymol. 413, 20-33
    • (2006) Methods Enzymol. , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 118
    • 0028121105 scopus 로고
    • Assembly of Alzheimer-like filaments from full-length tau protein
    • Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., and Goedert, M. (1994) Assembly of Alzheimer-like filaments from full-length tau protein FEBS Lett. 337, 135-138
    • (1994) FEBS Lett. , vol.337 , pp. 135-138
    • Crowther, R.A.1    Olesen, O.F.2    Smith, M.J.3    Jakes, R.4    Goedert, M.5
  • 119
    • 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, E. M., and 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
  • 120
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther, R. A., Olesen, O. F., Jakes, R., and Goedert, M. (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease FEBS Lett. 309, 199-202
    • (1992) FEBS Lett. , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 121
    • 70349155427 scopus 로고    scopus 로고
    • Tau aggregation followed by atomic force microscopy and surface plasmon resonance, and single molecule tau-tau interaction probed by atomic force spectroscopy
    • Barrantes, A., Sotres, J., Hernando-Perez, M., Benitez, M. J., de Pablo, P. J., Baro, A. M., Avila, J., and Jimenez, J. S. (2009) Tau aggregation followed by atomic force microscopy and surface plasmon resonance, and single molecule tau-tau interaction probed by atomic force spectroscopy J. Alzheimer's Dis. 18, 141-151
    • (2009) J. Alzheimer's Dis. , vol.18 , pp. 141-151
    • Barrantes, A.1    Sotres, J.2    Hernando-Perez, M.3    Benitez, M.J.4    De Pablo, P.J.5    Baro, A.M.6    Avila, J.7    Jimenez, J.S.8
  • 122
    • 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, E. M., and 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
  • 123
    • 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, D. M. and Binder, L. I. (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
  • 124
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (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
  • 125
    • 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, E. M., and 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
  • 126
    • 0038152836 scopus 로고    scopus 로고
    • Anionic micelles and vesicles induce tau fibrillization in vitro
    • Chirita, C. N., Necula, M., and 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
  • 127
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • Elbaum-Garfinkle, S., Ramlall, T., and 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
  • 128
    • 12144289142 scopus 로고    scopus 로고
    • Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers
    • Santa-Maria, I., Hernandez, F., Martin, C. P., Avila, J., and Moreno, F. J. (2004) Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers Biochemistry 43, 2888-2897
    • (2004) Biochemistry , vol.43 , pp. 2888-2897
    • Santa-Maria, I.1    Hernandez, F.2    Martin, C.P.3    Avila, J.4    Moreno, F.J.5
  • 129
    • 36348989570 scopus 로고    scopus 로고
    • Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-β-peptide aggregation
    • Santa-Maria, I., Hernandez, F., Moreno, F. J., and Avila, J. (2007) Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-β-peptide aggregation Neurosci. Lett. 429, 91-94
    • (2007) Neurosci. Lett. , vol.429 , pp. 91-94
    • Santa-Maria, I.1    Hernandez, F.2    Moreno, F.J.3    Avila, J.4
  • 130
    • 6344287664 scopus 로고    scopus 로고
    • Anionic contribution for fibrous maturation of protofibrillar assemblies of the human tau repeat domain in a fluoroalcohol solution
    • Konno, T., Oiki, S., Hasegawa, K., and Naiki, H. (2004) Anionic contribution for fibrous maturation of protofibrillar assemblies of the human tau repeat domain in a fluoroalcohol solution Biochemistry 43, 13613-13620
    • (2004) Biochemistry , vol.43 , pp. 13613-13620
    • Konno, T.1    Oiki, S.2    Hasegawa, K.3    Naiki, H.4
  • 131
    • 0023465163 scopus 로고
    • In vitro conditions for the self-polymerization of the microtubule-associated protein, tau factor
    • Montejo de Garcini, E. and Avila, J. (1987) In vitro conditions for the self-polymerization of the microtubule-associated protein, tau factor J. Biochem. 102, 1415-1421
    • (1987) J. Biochem. , vol.102 , pp. 1415-1421
    • Montejo De Garcini, E.1    Avila, J.2
  • 132
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S. and Mandelkow, E. (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments Biochemistry 41, 14885-14896
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 133
    • 4644342482 scopus 로고    scopus 로고
    • A static laser light scattering assay for surfactant-induced tau fibrillization
    • Necula, M. and Kuret, J. (2004) A static laser light scattering assay for surfactant-induced tau fibrillization Anal. Biochem. 333, 205-215
    • (2004) Anal. Biochem. , vol.333 , pp. 205-215
    • Necula, M.1    Kuret, J.2
  • 134
    • 17144395539 scopus 로고    scopus 로고
    • Triggers of full-length tau aggregation: A role for partially folded intermediates
    • Chirita, C. N., Congdon, E. E., Yin, H., and 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
  • 135
    • 1042299972 scopus 로고    scopus 로고
    • Evidence for an intermediate in tau filament formation
    • Chirita, C. N. and Kuret, J. (2004) Evidence for an intermediate in tau filament formation Biochemistry 43, 1704-1714
    • (2004) Biochemistry , vol.43 , pp. 1704-1714
    • Chirita, C.N.1    Kuret, J.2
  • 136
    • 0023187131 scopus 로고
    • Alzheimer's disease: Paired helical filaments and cytomembranes
    • Gray, E. G., Paula-Barbosa, M., and Roher, A. (1987) Alzheimer's disease: Paired helical filaments and cytomembranes Neuropathol. Appl. Neurobiol. 13, 91-110
    • (1987) Neuropathol. Appl. Neurobiol. , vol.13 , pp. 91-110
    • Gray, E.G.1    Paula-Barbosa, M.2    Roher, A.3
  • 137
    • 0033539689 scopus 로고    scopus 로고
    • Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression
    • King, M. E., Ahuja, V., Binder, L. I., and Kuret, J. (1999) Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression Biochemistry 38, 14851-14859
    • (1999) Biochemistry , vol.38 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 138
    • 80655128134 scopus 로고    scopus 로고
    • Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by tau protein
    • Ramachandran, G. and Udgaonkar, J. B. (2011) Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by tau protein J. Biol. Chem. 286, 38948-38959
    • (2011) J. Biol. Chem. , vol.286 , pp. 38948-38959
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 140
    • 77950473768 scopus 로고    scopus 로고
    • Quantitative characterization of heparin binding to tau protein: Implication for inducer-mediated tau filament formation
    • Zhu, H. L., Fernandez, C., Fan, J. B., Shewmaker, F., Chen, J., Minton, A. P., and Liang, Y. (2010) Quantitative characterization of heparin binding to tau protein: Implication for inducer-mediated tau filament formation J. Biol. Chem. 285, 3592-3599
    • (2010) J. Biol. Chem. , vol.285 , pp. 3592-3599
    • Zhu, H.L.1    Fernandez, C.2    Fan, J.B.3    Shewmaker, F.4    Chen, J.5    Minton, A.P.6    Liang, Y.7
  • 143
    • 84863983902 scopus 로고    scopus 로고
    • Evidence for the Existence of a Secondary Pathway for Fibril Growth during the Aggregation of Tau
    • Ramachandran, G. and Udgaonkar, J. B. (2012) Evidence for the Existence of a Secondary Pathway for Fibril Growth during the Aggregation of Tau J. Mol. Biol. 421, 296-314
    • (2012) J. Mol. Biol. , vol.421 , pp. 296-314
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 145
    • 84868104221 scopus 로고    scopus 로고
    • FTDP-17 Tau Mutations Induce Distinct Effects on Aggregation and Microtubule Interactions
    • Combs, B. and Gamblin, T. C. (2012) FTDP-17 Tau Mutations Induce Distinct Effects on Aggregation and Microtubule Interactions Biochemistry 51, 8597-8607
    • (2012) Biochemistry , vol.51 , pp. 8597-8607
    • Combs, B.1    Gamblin, T.C.2
  • 146
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • Morris, A. M., Watzky, M. A., Agar, J. N., and Finke, R. G. (2008) Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth Biochemistry 47, 2413-2427
    • (2008) Biochemistry , vol.47 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 147
    • 34547638452 scopus 로고    scopus 로고
    • Fiber-dependent amyloid formation as catalysis of an existing reaction pathway
    • Ruschak, A. M. and Miranker, A. D. (2007) Fiber-dependent amyloid formation as catalysis of an existing reaction pathway Proc. Natl. Acad. Sci. U.S.A. 104, 12341-12346
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12341-12346
    • Ruschak, A.M.1    Miranker, A.D.2
  • 148
    • 0842332840 scopus 로고    scopus 로고
    • Silent prions lying in wait: A two-hit model of prion/amyloid formation and infection
    • Hall, D. and Edskes, H. (2004) Silent prions lying in wait: A two-hit model of prion/amyloid formation and infection J. Mol. Biol. 336, 775-786
    • (2004) J. Mol. Biol. , vol.336 , pp. 775-786
    • Hall, D.1    Edskes, H.2
  • 149
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S. R., Douglass, A., Vale, R. D., and Weissman, J. S. (2004) Mechanism of prion propagation: Amyloid growth occurs by monomer addition PLoS Biol. 2, e321
    • (2004) PLoS Biol. , vol.2 , pp. 321
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 150
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue, W. F., Homans, S. W., and Radford, S. E. (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly Proc. Natl. Acad. Sci. U.S.A. 105, 8926-8931
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 151
    • 28844482969 scopus 로고    scopus 로고
    • The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
    • Librizzi, F. and Rischel, C. (2005) The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways Protein Sci. 14, 3129-3134
    • (2005) Protein Sci. , vol.14 , pp. 3129-3134
    • Librizzi, F.1    Rischel, C.2
  • 152
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26, 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 154
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S., Zheng-Fischhofer, Q., Ackmann, M., Biernat, J., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias Biochemistry 39, 11714-11721
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 155
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin, T. C., King, M. E., Dawson, H., Vitek, M. P., Kuret, J., Berry, R. W., and Binder, L. I. (2000) In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants Biochemistry 39, 6136-6144
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 156
    • 0032919462 scopus 로고    scopus 로고
    • Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
    • Goedert, M., Jakes, R., and Crowther, R. A. (1999) Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments FEBS Lett. 450, 306-311
    • (1999) FEBS Lett. , vol.450 , pp. 306-311
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 157
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju, P., Lewis, J., Easson, C., Yen, S., Hackett, J., Hutton, M., and Yen, S. H. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations FEBS Lett. 447, 195-199
    • (1999) FEBS Lett. , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 158
    • 54349085644 scopus 로고    scopus 로고
    • Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps
    • Chang, E., Kim, S., Yin, H., Nagaraja, H. N., and Kuret, J. (2008) Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps J. Neurochem. 107, 1113-1123
    • (2008) J. Neurochem. , vol.107 , pp. 1113-1123
    • Chang, E.1    Kim, S.2    Yin, H.3    Nagaraja, H.N.4    Kuret, J.5
  • 161
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass, C. and Selkoe, D. J. (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
  • 164
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., and Davies, P. (2005) Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms J. Neurosci. 25, 5446-5454
    • (2005) J. Neurosci. , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 166
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
    • Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., and Takashima, A. (2006) Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease Neurosci. Res. 54, 197-201
    • (2006) Neurosci. Res. , vol.54 , pp. 197-201
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, S.4    Ikai, A.5    Takashima, A.6
  • 169
    • 47249159078 scopus 로고    scopus 로고
    • A soluble oligomer of tau associated with fiber formation analyzed by NMR
    • Peterson, D. W., Zhou, H., Dahlquist, F. W., and Lew, J. (2008) A soluble oligomer of tau associated with fiber formation analyzed by NMR Biochemistry 47, 7393-7404
    • (2008) Biochemistry , vol.47 , pp. 7393-7404
    • Peterson, D.W.1    Zhou, H.2    Dahlquist, F.W.3    Lew, J.4
  • 171
    • 77953341846 scopus 로고    scopus 로고
    • Mechanisms of amyloid fibril formation by proteins
    • Kumar, S. and Udgaonkar, J. B. (2010) Mechanisms of amyloid fibril formation by proteins Curr. Sci. 98, 639-656
    • (2010) Curr. Sci. , vol.98 , pp. 639-656
    • Kumar, S.1    Udgaonkar, J.B.2
  • 172
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-β fibril polymorphisms
    • Goldsbury, C., Frey, P., Olivieri, V., Aebi, U., and Muller, S. A. (2005) Multiple assembly pathways underlie amyloid-β fibril polymorphisms J. Mol. Biol. 352, 282-298
    • (2005) J. Mol. Biol. , vol.352 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Muller, S.A.5
  • 174
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid
    • Gosal, W. S., Morten, I. J., Hewitt, E. W., Smith, D. A., Thomson, N. H., and Radford, S. E. (2005) Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid J. Mol. Biol. 351, 850-864
    • (2005) J. Mol. Biol. , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 177
    • 0029997922 scopus 로고    scopus 로고
    • Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease
    • Mena, R., Edwards, P. C., Harrington, C. R., Mukaetova-Ladinska, E. B., and Wischik, C. M. (1996) Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease Acta Neuropathol. 91, 633-641
    • (1996) Acta Neuropathol. , vol.91 , pp. 633-641
    • Mena, R.1    Edwards, P.C.2    Harrington, C.R.3    Mukaetova-Ladinska, E.B.4    Wischik, C.M.5
  • 178
    • 0034843039 scopus 로고    scopus 로고
    • Sequence of neurofibrillary changes in aging and Alzheimer's disease: A confocal study with phospho-tau antibody, AD2
    • Galvan, M., David, J. P., Delacourte, A., Luna, J., and Mena, R. (2001) Sequence of neurofibrillary changes in aging and Alzheimer's disease: A confocal study with phospho-tau antibody, AD2 J. Alzheimer's Dis. 3, 417-425
    • (2001) J. Alzheimer's Dis. , vol.3 , pp. 417-425
    • Galvan, M.1    David, J.P.2    Delacourte, A.3    Luna, J.4    Mena, R.5
  • 179
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak, E., Braak, H., and Mandelkow, E. M. (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
  • 180
    • 0021344498 scopus 로고
    • Alzheimer paired helical filaments: Bulk isolation, solubility, and protein composition
    • Iqbal, K., Zaidi, T., Thompson, C. H., Merz, P. A., and Wisniewski, H. M. (1984) Alzheimer paired helical filaments: Bulk isolation, solubility, and protein composition Acta Neuropathol. 62, 167-177
    • (1984) Acta Neuropathol. , vol.62 , pp. 167-177
    • Iqbal, K.1    Zaidi, T.2    Thompson, C.H.3    Merz, P.A.4    Wisniewski, H.M.5
  • 183
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi, A. and 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
  • 184
    • 84863808563 scopus 로고    scopus 로고
    • Prion-like spread of protein aggregates in neurodegeneration
    • Polymenidou, M. and Cleveland, D. W. (2012) Prion-like spread of protein aggregates in neurodegeneration J. Exp. Med. 209, 889-893
    • (2012) J. Exp. Med. , vol.209 , pp. 889-893
    • Polymenidou, M.1    Cleveland, D.W.2
  • 185
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L., and Diamond, M. I. (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
  • 188
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of tau aggregation by fibrillar species
    • Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., and Diamond, M. I. (2012) Trans-cellular propagation of tau aggregation by fibrillar species J. Biol. Chem. 287, 19440-19451
    • (2012) J. Biol. Chem. , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 190
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H., and Diamond, M. I. (2009) Conformational diversity of wild-type tau fibrils specified by templated conformation change J. Biol. Chem. 284, 3546-3551
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 198
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 200
    • 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, D. P., and Anderton, B. H. (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
  • 201
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between fyn and tau
    • Bhaskar, K., Yen, S. H., and 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
  • 205
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., and Hasegawa, M. (2005) Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins J. Biol. Chem. 280, 7614-7623
    • (2005) J. Biol. Chem. , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 208
    • 51349134160 scopus 로고    scopus 로고
    • Hope in Alzheimer's fight emerges from unexpected places
    • Gura, T. (2008) Hope in Alzheimer's fight emerges from unexpected places Nat. Med. 14, 894
    • (2008) Nat. Med. , vol.14 , pp. 894
    • Gura, T.1


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