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Volumn 289, Issue 49, 2014, Pages 34389-34407

Oligomer formation of tau protein hyperphosphorylated in cells

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CYTOLOGY; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES; OLIGOMERS; PROTEINS;

EID: 84917706097     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.611368     Document Type: Article
Times cited : (114)

References (87)
  • 1
    • 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., Preuss, U., Mandelkow, E. M., and 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
  • 2
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff, W. H., and Johnson, G. V. (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
  • 3
    • 0027361281 scopus 로고
    • Microtubule-associated protein Tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., and 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
    • Köpke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 4
    • 0026676007 scopus 로고
    • Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments
    • Ksiezak-Reding, H., Liu, W. K., and Yen, S. H. (1992) Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments. Brain Res. 597, 209-219
    • (1992) Brain Res. , vol.597 , pp. 209-219
    • Ksiezak-Reding, H.1    Liu, W.K.2    Yen, S.H.3
  • 5
    • 0026134421 scopus 로고
    • Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
    • Braak, H., and Braak, E. (1991) Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections. Brain Pathol. 1, 213-216
    • (1991) Brain Pathol. , vol.1 , pp. 213-216
    • Braak, H.1    Braak, E.2
  • 6
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V. M., and Trojanowski, J. Q. (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
  • 10
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso, A., Zaidi, T., Novak, M., Grundke-Iqbal, I., and Iqbal, K. (2001) Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl. Acad. Sci. U.S.A. 98, 6923-6928
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 11
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo, E. S., Shin, R. W., Billingsley, M. L., Van deVoorde, A., O'Connor, M., Trojanowski, J. Q., and Lee, V. M. (1994) Biopsy-derived 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
  • 13
    • 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., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., and Härtig, 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    Rüdiger, J.5    Van Der Zee, E.A.6    Harkany, T.7    Holzer, M.8    Härtig, W.9
  • 14
    • 0031928259 scopus 로고    scopus 로고
    • Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease
    • Preuss, U., and Mandelkow, E. M. (1998) Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease. Eur. J. Cell Biol. 76, 176-184
    • (1998) Eur. J. Cell Biol. , vol.76 , pp. 176-184
    • Preuss, U.1    Mandelkow, E.M.2
  • 15
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease?
    • Vincent, I., Rosado, M., and Davies, P. (1996) Mitotic mechanisms in Alzheimer's disease? J. Cell Biol. 132, 413-425
    • (1996) J. Cell Biol. , vol.132 , pp. 413-425
    • Vincent, I.1    Rosado, M.2    Davies, P.3
  • 16
    • 0027372016 scopus 로고
    • The extent of phosphorylation of fetal tau is comparable with that of PHF-tau from Alzheimer paired helical filaments
    • Kenessey, A., and Yen, S. H. (1993) The extent of phosphorylation of fetal tau is comparable with that of PHF-tau from Alzheimer paired helical filaments. Brain Res. 629, 40-46
    • (1993) Brain Res. , vol.629 , pp. 40-46
    • Kenessey, A.1    Yen, S.H.2
  • 17
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
    • Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. J. Biol. Chem. 267, 17047-17054
    • (1992) J. Biol. Chem. , vol.267 , pp. 17047-17054
    • Hasegawa, M.1    Morishima-Kawashima, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 18
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H., and Noble, W. (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 24
    • 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., and Mandelkow, E. M. (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
  • 25
    • 0025788253 scopus 로고
    • Processes induced by tau expression in Sf9 cells have an axon-like microtubule organization
    • Baas, P. W., Pienkowski, T. P., and Kosik, K. S. (1991) Processes induced by tau expression in Sf9 cells have an axon-like microtubule organization. J. Cell Biol. 115, 1333-1344
    • (1991) J. Cell Biol. , vol.115 , pp. 1333-1344
    • Baas, P.W.1    Pienkowski, T.P.2    Kosik, K.S.3
  • 26
    • 0032935412 scopus 로고    scopus 로고
    • The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains
    • Biernat, J., and Mandelkow, E. M. (1999) The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains. Mol. Biol. Cell 10, 727-740
    • (1999) Mol. Biol. Cell , vol.10 , pp. 727-740
    • Biernat, J.1    Mandelkow, E.M.2
  • 27
    • 0028229455 scopus 로고
    • Microtubule-associated protein function: Lessons from expression in Spodoptera frugiperda cells
    • Kosik, K. S., and McConlogue, L. (1994) Microtubule-associated protein function: lessons from expression in Spodoptera frugiperda cells. Cell Motil. Cytoskeleton 28, 195-198
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 195-198
    • Kosik, K.S.1    McConlogue, L.2
  • 28
    • 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, E. M., and 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
  • 29
    • 0025020967 scopus 로고
    • Cell volume increase in Escherichia coli after shifts to richer media
    • Kubitschek, H. E. (1990) Cell volume increase in Escherichia coli after shifts to richer media. J. Bacteriol. 172, 94-101
    • (1990) J. Bacteriol. , vol.172 , pp. 94-101
    • Kubitschek, H.E.1
  • 30
    • 84917708048 scopus 로고    scopus 로고
    • (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds) 5th Ed., John Wiley & Sons, Inc., New York
    • Ausubel, F. M. (2002) in Short Protocols in Molecular Biology (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds) 5th Ed., p. 625, John Wiley & Sons, Inc., New York
    • (2002) Short Protocols in Molecular Biology , pp. 625
    • Ausubel, F.M.1
  • 31
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg, S. G., and Davies, P. (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc. Natl. Acad. Sci. U.S.A. 87, 5827-5831
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 32
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
    • Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., and Mandelkow, E. M. (2013) Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin. EMBO J. 32, 2920-2937
    • (2013) EMBO J. , vol.32 , pp. 2920-2937
    • Zempel, H.1    Luedtke, J.2    Kumar, Y.3    Biernat, J.4    Dawson, H.5    Mandelkow, E.6    Mandelkow, E.M.7
  • 33
    • 0000408582 scopus 로고
    • Near infrared spark source excitation for fluorescence lifetime measurements
    • Birch, D. J., Hungerford, G., and Imhof, R. E. (1991) Near infrared spark source excitation for fluorescence lifetime measurements. Rev. Sci. Instrum. 62, 2405
    • (1991) Rev. Sci. Instrum. , vol.62 , pp. 2405
    • Birch, D.J.1    Hungerford, G.2    Imhof, R.E.3
  • 34
    • 24644483798 scopus 로고    scopus 로고
    • Efficient uniform isotope labeling of Abl kinase expressed in baculovirus-infected insect cells
    • Strauss, A., Bitsch, F., Fendrich, G., Graff, P., Knecht, R., Meyhack, B., and Jahnke, W. (2005) Efficient uniform isotope labeling of Abl kinase expressed in baculovirus-infected insect cells. J. Biomol. NMR 31, 343-349
    • (2005) J. Biomol. NMR , vol.31 , pp. 343-349
    • Strauss, A.1    Bitsch, F.2    Fendrich, G.3    Graff, P.4    Knecht, R.5    Meyhack, B.6    Jahnke, W.7
  • 35
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • Sivashanmugam, A., Murray, V., Cui, C., Zhang, Y., Wang, J., and Li, Q. (2009) Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci. 18, 936-948
    • (2009) Protein Sci. , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5    Li, Q.6
  • 36
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee, V. M., Balin, B. J., Otvos, L., Jr., and Trojanowski, J. Q. (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251, 675-678
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 37
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphory- lation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J., and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphory- lation of all six brain isoforms. Neuron 8, 159-168
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 38
    • 0026663076 scopus 로고
    • Phosphorylated baculovirus p10 is a heat-stable microtubule-associated protein associated with process formation in Sf9 cells
    • Cheley, S., Kosik, K. S., Paskevich, P., Bakalis, S., and Bayley, H. (1992) Phosphorylated baculovirus p10 is a heat-stable microtubule-associated protein associated with process formation in Sf9 cells. J. Cell Sci. 102, 739-752
    • (1992) J. Cell Sci. , vol.102 , pp. 739-752
    • Cheley, S.1    Kosik, K.S.2    Paskevich, P.3    Bakalis, S.4    Bayley, H.5
  • 39
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis, D., and Lovrien, R. (1998) 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74, 422-429
    • (1998) Biophys. J. , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 40
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., III (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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
  • 44
    • 0001966229 scopus 로고    scopus 로고
    • (Lakowicz, J. R., ed) Kluwer Academics, New York
    • Steiner, R. F. (1999) in Topics in Fluorescence Spectroscopy (Lakowicz, J. R., ed) pp. 1-52, Kluwer Academics, New York
    • (1999) Topics in Fluorescence Spectroscopy , pp. 1-52
    • Steiner, R.F.1
  • 48
    • 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., and Mandelkow, E. (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
  • 50
    • 48749125392 scopus 로고    scopus 로고
    • β-Lactoglobulin assembles into amyloid through sequential aggregated intermediates
    • Giurleo, J. T., He, X., and Talaga, D. S. (2008) β-Lactoglobulin assembles into amyloid through sequential aggregated intermediates. J. Mol. Biol. 381, 1332-1348
    • (2008) J. Mol. Biol. , vol.381 , pp. 1332-1348
    • Giurleo, J.T.1    He, X.2    Talaga, D.S.3
  • 52
    • 0021334090 scopus 로고
    • Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes
    • Drubin, D. G., Caput, D., and Kirschner, M. W. (1984) Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes. J. Cell Biol. 98, 1090-1097
    • (1984) J. Cell Biol. , vol.98 , pp. 1090-1097
    • Drubin, D.G.1    Caput, D.2    Kirschner, M.W.3
  • 53
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso, A. C., Grundke-Iqbal, I., and Iqbal, K. (1996) Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat. Med. 2, 783-787
    • (1996) Nat. Med. , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 55
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 15, 349-357
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 56
    • 78650861616 scopus 로고    scopus 로고
    • Tau aggregation is a therapeutic target for Alzheimer's disease
    • Takashima, A. (2010) Tau aggregation is a therapeutic target for Alzheimer's disease. Curr. Alzheimer Res. 7, 665-669
    • (2010) Curr. Alzheimer Res. , vol.7 , pp. 665-669
    • Takashima, A.1
  • 58
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai, H. C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., and Hyman, B. T. (2012) The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am. J. Pathol. 181, 1426-1435
    • (2012) Am. J. Pathol. , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 60
    • 0018149343 scopus 로고
    • Radioimmunoassay for tubulin: A quantitative comparison of the tubulin content of different established tissue culture cells and tissues
    • Hiller, G., and 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
  • 61
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina, L. A., Cooper, E. M., Uversky, V. N., and Fink, A. L. (2004) The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 17, 456-464
    • (2004) J. Mol. Recognit. , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4
  • 62
    • 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, E. M., and 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
  • 65
    • 34547203592 scopus 로고    scopus 로고
    • Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model
    • Wang, Y. P., Biernat, J., Pickhardt, M., Mandelkow, E., and Mandelkow, E. M. (2007) Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model. Proc. Natl. Acad. Sci. U.S.A. 104, 10252-10257
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10252-10257
    • Wang, Y.P.1    Biernat, J.2    Pickhardt, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 66
    • 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
    • Schweers, O., Mandelkow, E. M., Biernat, J., and 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. U.S.A. 92, 8463-8467
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 67
    • 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
  • 68
    • 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
  • 69
    • 77950473768 scopus 로고    scopus 로고
    • Quantitative characterization of heparin binding to Tau protein: Implication for inducer-mediated Tau filament formation
    • Zhu, H. L., Fernández, 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    Fernández, C.2    Fan, J.B.3    Shewmaker, F.4    Chen, J.5    Minton, A.P.6    Liang, Y.7
  • 71
    • 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
  • 73
    • 84860373672 scopus 로고    scopus 로고
    • FLEXIQinase, a mass spectrometry-based assay, to unveil multikinase mechanisms
    • Singh, S. A., Winter, D., Bilimoria, P. M., Bonni, A., Steen, H., and Steen, J. A. (2012) FLEXIQinase, a mass spectrometry-based assay, to unveil multikinase mechanisms. Nat. Methods 9, 504-508
    • (2012) Nat. Methods , vol.9 , pp. 504-508
    • Singh, S.A.1    Winter, D.2    Bilimoria, P.M.3    Bonni, A.4    Steen, H.5    Steen, J.A.6
  • 74
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding
    • Cho, J. H., and Johnson, G. V. (2003) Glycogen synthase kinase 3β phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J. Biol. Chem. 278, 187-193
    • (2003) J. Biol. Chem. , vol.278 , pp. 187-193
    • Cho, J.H.1    Johnson, G.V.2
  • 75
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein
    • Eidenmüller, J., Fath, T., Maas, T., Pool, M., Sontag, E., and Brandt, R. (2001) Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. Biochem. J. 357, 759-767
    • (2001) Biochem. J. , vol.357 , pp. 759-767
    • Eidenmüller, J.1    Fath, T.2    Maas, T.3    Pool, M.4    Sontag, E.5    Brandt, R.6
  • 76
    • 1642280378 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau protein alters its ability for self-aggregation
    • Haase, C., Stieler, J. T., Arendt, T., and Holzer, M. (2004) Pseudophosphorylation of tau protein alters its ability for self-aggregation. J. Neurochem. 88, 1509-1520
    • (2004) J. Neurochem. , vol.88 , pp. 1509-1520
    • Haase, C.1    Stieler, J.T.2    Arendt, T.3    Holzer, M.4
  • 77
  • 78
    • 58049214009 scopus 로고    scopus 로고
    • Tau oligomerization: A role for tau aggregation intermediates linked to neurodegeneration
    • Sahara, N., Maeda, S., and Takashima, A. (2008) Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration. Curr. Alzheimer Res. 5, 591-598
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 591-598
    • Sahara, N.1    Maeda, S.2    Takashima, A.3
  • 81
    • 0021673482 scopus 로고
    • Involvement of the carboxyl-terminal domain of tubulin in the regulation of its assembly
    • Serrano, L., de la Torre, J., Maccioni, R. B., and Avila, J. (1984) Involvement of the carboxyl-terminal domain of tubulin in the regulation of its assembly. Proc. Natl. Acad. Sci. U.S.A. 81, 5989-5993
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 5989-5993
    • Serrano, L.1    De La Torre, J.2    Maccioni, R.B.3    Avila, J.4
  • 82
  • 83
    • 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
  • 84
    • 79251563831 scopus 로고    scopus 로고
    • The physiological link between metabolic rate depression and tau phosphorylation in mammalian hibernation
    • Stieler, J. T., Bullmann, T., Kohl, F., Tøien, Ø., Brückner, M. K., Härtig, W., Barnes, B. M., and Arendt, T. (2011) The physiological link between metabolic rate depression and tau phosphorylation in mammalian hibernation. PLoS One 6, e14530
    • (2011) PLoS One , vol.6 , pp. e14530
    • Stieler, J.T.1    Bullmann, T.2    Kohl, F.3    Tøien, O.4    Brückner, M.K.5    Härtig, W.6    Barnes, B.M.7    Arendt, T.8
  • 87
    • 33646246733 scopus 로고    scopus 로고
    • HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites
    • Dickey, C. A., Dunmore, J., Lu, B., Wang, J. W., Lee, W. C., Kamal, A., Burrows, F., Eckman, C., Hutton, M., and Petrucelli, L. (2006) HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites. FASEB J. 20, 753-755
    • (2006) FASEB J. , vol.20 , pp. 753-755
    • Dickey, C.A.1    Dunmore, J.2    Lu, B.3    Wang, J.W.4    Lee, W.C.5    Kamal, A.6    Burrows, F.7    Eckman, C.8    Hutton, M.9    Petrucelli, L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.