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Volumn 26, Issue 7-8, 2006, Pages 1085-1097

Intrinsically disordered proteins in the neurodegenerative processes: Formation of tau protein paired helical filaments and their analysis

Author keywords

Alzheimer's disease; Intrinsically disordered proteins; Monoclonal antibody; Neurodegeneration; Neurofibrillary pathology; Paired helical filaments; Tau protein

Indexed keywords

ALPHA SYNUCLEIN; INTRINSICALLY DISORDERED PROTEIN; MONOCLONAL ANTIBODY; POLYPEPTIDE; PRION PROTEIN; PROTEIN; TAU PROTEIN;

EID: 33845524844     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10571-006-9083-3     Document Type: Review
Times cited : (64)

References (100)
  • 1
  • 2
    • 0034730759 scopus 로고    scopus 로고
    • Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
    • Ackmann, M., Wiech, H., 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
  • 3
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • Alonso, A., Mederlyova, A., Novak, M., Grundke-Iqbal, I., and Iqbal, K. (2004). Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J. Biol. Chem. 279:34873-34881.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34873-34881
    • Alonso, A.1    Mederlyova, A.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 4
    • 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
  • 5
    • 0033731782 scopus 로고    scopus 로고
    • Are denatured proteins ever random coils?
    • Baldwin, R. L., and Zimm, B. H. (2000). Are denatured proteins ever random coils? Proc. Natl. Acad. Sci. U.S.A. 97:12391-12392.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12391-12392
    • Baldwin, R.L.1    Zimm, B.H.2
  • 6
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-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 beta-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
  • 7
    • 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
  • 8
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta 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-beta 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
  • 10
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H., and Braak, E. (1991). Neuropathological stageing of Alzheimer-related changes. Acta. Neuropathol. (Berl.) 82:239-259.
    • (1991) Acta. Neuropathol. (Berl.) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0028121105 scopus 로고
    • Assembly of Alzheimerlike filaments from full-length tau protein
    • Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., and Goedert, M. (1994). Assembly of Alzheimerlike 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
  • 15
    • 0022980104 scopus 로고
    • Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte, A., and Defossez, A. (1986). Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J. Neurol. Sci. 76:173-186.
    • (1986) J. Neurol. Sci. , vol.76 , pp. 173-186
    • Delacourte, A.1    Defossez, A.2
  • 18
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002). Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12:54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005a). Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell. Biol. 6:197-208.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson, H. J., and Wright, P. E. (2005b). Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394:299-321.
    • (2005) Methods Enzymol. , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 21
    • 12344328360 scopus 로고    scopus 로고
    • Residual structure in the repeat domain of tau: Echoes of microtubule binding and paired helical filament formation
    • Eliezer, D., Barre, P., Kobaslija, M., Chan, D., Li, X., and Heend, L. (2005). Residual structure in the repeat domain of tau: Echoes of microtubule binding and paired helical filament formation. Biochemistry 44:1026-1036.
    • (2005) Biochemistry , vol.44 , pp. 1026-1036
    • Eliezer, D.1    Barre, P.2    Kobaslija, M.3    Chan, D.4    Li, X.5    Heend, L.6
  • 22
    • 10944256690 scopus 로고    scopus 로고
    • Inability of tau to properly regulate neuronal microtubule dynamics: A loss-of-function mechanism by which tau might mediate neuronal cell death
    • Feinstein, S. C., and Wilson, L. (2005). Inability of tau to properly regulate neuronal microtubule dynamics: A loss-of-function mechanism by which tau might mediate neuronal cell death. Biochim. Biophys. Acta 1739:268-279.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 268-279
    • Feinstein, S.C.1    Wilson, L.2
  • 23
    • 0037432188 scopus 로고    scopus 로고
    • Protein folding: Could hydrophobic collapse be coupled with hydrogen-bond formation?
    • Fernandez, A., Kardos, J., and Goto, Y. (2003). Protein folding: Could hydrophobic collapse be coupled with hydrogen-bond formation? FEBS Lett. 536:187-192.
    • (2003) FEBS Lett. , vol.536 , pp. 187-192
    • Fernandez, A.1    Kardos, J.2    Goto, Y.3
  • 24
    • 0037422589 scopus 로고    scopus 로고
    • Insufficiently dehydrated hydrogen bonds as determinants of protein interactions
    • Fernandez, A., and Scheraga, H. A. (2003). Insufficiently dehydrated hydrogen bonds as determinants of protein interactions. Proc. Natl. Acad. Sci. U.S.A. 100:113-118.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 113-118
    • Fernandez, A.1    Scheraga, H.A.2
  • 25
    • 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
  • 26
    • 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. (1998a). 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
  • 28
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P., and Tompa, P. (2004). Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 338:1015-1026.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 29
    • 11144321178 scopus 로고    scopus 로고
    • Potential structure/function relationships of predicted secondary structural elements of tau
    • Gamblin, T. C. (2005). Potential structure/function relationships of predicted secondary structural elements of tau. Biochim. Biophys. Acta 1739:140-149.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 140-149
    • Gamblin, T.C.1
  • 30
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003a). Modeling tau polymerization in vitro: A review and synthesis. Biochemistry 42:15009-15017.
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 31
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003b). Tau polymerization: Role of the amino terminus. Biochemistry 42:2252-2257.
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 32
    • 0034700253 scopus 로고    scopus 로고
    • Oxidative regulation of fatty acid-induced tau polymerization
    • Gamblin, T. C., King, M. E., Kuret, J., Berry, R. W., and Binder, L. I. (2000). Oxidative regulation of fatty acid-induced tau polymerization. Biochemistry 39:14203-14210.
    • (2000) Biochemistry , vol.39 , pp. 14203-14210
    • Gamblin, T.C.1    King, M.E.2    Kuret, J.3    Berry, R.W.4    Binder, L.I.5
  • 33
    • 0342368728 scopus 로고    scopus 로고
    • The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old
    • Garcia-Sierra, F., Hauw, J. J., Duyckaerts, C., Wischik, C. M., Luna-Munoz, J., and Mena, R. (2000). The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old. Acta Neuropathol. (Berl.) 100:29-35.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 29-35
    • Garcia-Sierra, F.1    Hauw, J.J.2    Duyckaerts, C.3    Wischik, C.M.4    Luna-Munoz, J.5    Mena, R.6
  • 36
    • 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
  • 37
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989). Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3:519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 38
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with proteinprotein interactions
    • Goh, C. S., Milburn, D., and Gerstein, M. (2004). Conformational changes associated with proteinprotein interactions. Curr. Opin. Struct. Biol. 14:104-109.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 104-109
    • Goh, C.S.1    Milburn, D.2    Gerstein, M.3
  • 39
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • Gong, C. X., Liu, F., Grundke-Iqbal, I., and Iqbal, K. (2005). Post-translational modifications of tau protein in Alzheimer's disease. J. Neural Transm. 112:813-838.
    • (2005) J. Neural Transm. , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 40
    • 0037137228 scopus 로고    scopus 로고
    • The conformations of filamentous and soluble tau associated with Alzheimer paired helical filaments
    • Goux, W. J. (2002). The conformations of filamentous and soluble tau associated with Alzheimer paired helical filaments. Biochemistry 41:13798-13806.
    • (2002) Biochemistry , vol.41 , pp. 13798-13806
    • Goux, W.J.1
  • 41
    • 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
  • 42
  • 44
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • Gunasekaran, K., Tsai, C. J., and Nussinov, R. (2004). Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J. Mol. Biol. 341:1327-1341.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 48
    • 0025785076 scopus 로고
    • Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease
    • Jakes, R., Novak, M., Davison, M., and Wischik, C. M. (1991). Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO J. 10:2725-2729.
    • (1991) EMBO J. , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 50
    • 0033558929 scopus 로고    scopus 로고
    • Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
    • Jicha, G. A., Berenfeld, B., and Davies, P. (1999). Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease. J. Neurosci. Res. 55:713-723.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 713-723
    • Jicha, G.A.1    Berenfeld, B.2    Davies, P.3
  • 51
    • 0030783142 scopus 로고    scopus 로고
    • A conformation-and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha, G. A., Lane, E., Vincent, I., Otvos, L., Jr., Hoffmann, R., and Davies, P. (1997). A conformation-and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J. Neurochem. 69:2087-2095.
    • (1997) J. Neurochem. , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos Jr., L.4    Hoffmann, R.5    Davies, P.6
  • 52
    • 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
  • 54
    • 0034023751 scopus 로고    scopus 로고
    • Differential assembly of human tau isoforms in the presence of arachidonic acid
    • King, M. E., Gamblin, T. C., Kuret, J., and Binder, L. I. (2000). Differential assembly of human tau isoforms in the presence of arachidonic acid. J. Neurochem. 74:1749-1757.
    • (2000) J. Neurochem. , vol.74 , pp. 1749-1757
    • King, M.E.1    Gamblin, T.C.2    Kuret, J.3    Binder, L.I.4
  • 55
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation
    • Kirschner, D. A., Abraham, C., and Selkoe, D. J. (1986). X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation. Proc. Natl. Acad. Sci. U.S.A. 83:503-507.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 56
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke, 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
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 58
    • 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
  • 61
    • 0041355331 scopus 로고    scopus 로고
    • Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies
    • Makrides, V., Shen, T. E., Bhatia, R., Smith, B. L., Thimm, J., Lal, R., and Feinstein, S. C. (2003). Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies. J. Biol. Chem. 278:33298-33304.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33298-33304
    • Makrides, V.1    Shen, T.E.2    Bhatia, R.3    Smith, B.L.4    Thimm, J.5    Lal, R.6    Feinstein, S.C.7
  • 62
    • 0036290512 scopus 로고    scopus 로고
    • Amphipathic helical behavior of the third repeat fragment in the taumicrotubule-binding domain, studied by (1)H NMR spectroscopy
    • Minoura, K., Tomoo, K., Ishida, T., Hasegawa, H., Sasaki, M., and Taniguchi, T. (2002). Amphipathic helical behavior of the third repeat fragment in the taumicrotubule-binding domain, studied by (1)H NMR spectroscopy. Biochem. Biophys. Res. Commun. 294:210-214.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 210-214
    • Minoura, K.1    Tomoo, K.2    Ishida, T.3    Hasegawa, H.4    Sasaki, M.5    Taniguchi, T.6
  • 63
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions
    • Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., and Zweckstetter, M. (2005). Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions. J. Biol. Chem. 280:24978-24986.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 64
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • Novak, M., Jakes, R., Edwards, P. C., Milstein, C., and Wischik, C. M. (1991). Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc. Natl. Acad. Sci. U.S.A. 88:5837-5841.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 65
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak, M., Kabat, J., and Wischik, C. M. (1993). Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 12:365-370.
    • (1993) EMBO J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 67
    • 0024814559 scopus 로고
    • Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF
    • Novak, M., Wischik, C. M., Edwards, P., Pannell, R., and Milstein, C. (1989). Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF. Prog. Clin. Biol. Res. 317:755-761.
    • (1989) Prog. Clin. Biol. Res. , vol.317 , pp. 755-761
    • Novak, M.1    Wischik, C.M.2    Edwards, P.3    Pannell, R.4    Milstein, C.5
  • 68
    • 0036280798 scopus 로고    scopus 로고
    • Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17
    • Pollesello, P., and Annila, A. (2002). Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17. Biophys. J. 83:484-490.
    • (2002) Biophys. J. , vol.83 , pp. 484-490
    • Pollesello, P.1    Annila, A.2
  • 69
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and Poirier, M. A. (2004). Protein aggregation and neurodegenerative disease. Nat. Med. 10(Suppl):S10-S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 70
    • 0028912146 scopus 로고
    • Alzheimer paired helical filaments, untreated and pronase digested, studied by vertical platinum-carbon replication and high resolution transmission electron microscopy
    • Ruben, G. C., Novak, M., Edwards, P. C., and Iqbal, K. (1995). Alzheimer paired helical filaments, untreated and pronase digested, studied by vertical platinum-carbon replication and high resolution transmission electron microscopy. Brain Res. 675:1-12.
    • (1995) Brain Res. , vol.675 , pp. 1-12
    • Ruben, G.C.1    Novak, M.2    Edwards, P.C.3    Iqbal, K.4
  • 72
    • 0032554636 scopus 로고    scopus 로고
    • Role of phosphorylation in determining the backbone dynamics of the serine/threonineproline motif and Pin1 substrate recognition
    • Schutkowski, M., Bernhardt, A., Zhou, X. Z., Shen, M., Reimer, U., Rahfeld, J. U., Lu, K. P., and Fischer, G. (1998). Role of phosphorylation in determining the backbone dynamics of the serine/threonineproline motif and Pin1 substrate recognition. Biochemistry 37:5566-5575.
    • (1998) Biochemistry , vol.37 , pp. 5566-5575
    • Schutkowski, M.1    Bernhardt, A.2    Zhou, X.Z.3    Shen, M.4    Reimer, U.5    Rahfeld, J.U.6    Lu, K.P.7    Fischer, G.8
  • 73
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-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 beta-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
  • 74
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi, Z., Woody, R. W., and Kallenbach, N. R. (2002). Is polyproline II a major backbone conformation in unfolded proteins? Adv. Protein Chem. 62:163-240.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 75
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A., Portman, J. J., and Wolynes, P. G. (2000). Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 97:8868-8873.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 76
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle, D., and Ackerman, M. S. (2001). Persistence of native-like topology in a denatured protein in 8 M urea. Science 293:487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 78
    • 27144528728 scopus 로고    scopus 로고
    • Disordered p27(Kip1) exhibits intrinsic structure resembling the Cdk2/Cyclin A-bound conformation
    • Sivakolundu, S. G., Bashford, D., and Kriwacki, R. W. (2005). Disordered p27(Kip1) exhibits intrinsic structure resembling the Cdk2/Cyclin A-bound conformation. J. Mol. Biol. 353:1118-1128.
    • (2005) J. Mol. Biol. , vol.353 , pp. 1118-1128
    • Sivakolundu, S.G.1    Bashford, D.2    Kriwacki, R.W.3
  • 79
    • 33845541863 scopus 로고    scopus 로고
    • Tau protein fragment derived from the core PHF behaves as natively unfolded upon dimerization
    • Skrabana, R., Csokova, N., Liebig, H. D., Smrzka, O., and Novak, M. (2004a). Tau protein fragment derived from the core PHF behaves as natively unfolded upon dimerization. Neurobiol. Aging 25:S425.
    • (2004) Neurobiol. Aging , vol.25
    • Skrabana, R.1    Csokova, N.2    Liebig, H.D.3    Smrzka, O.4    Novak, M.5
  • 80
    • 2942594301 scopus 로고    scopus 로고
    • Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423
    • Skrabana, R., Kontsek, P., Mederlyova, A., Iqbal, K., and Novak, M. (2004b). Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS Lett. 568:178-182.
    • (2004) FEBS Lett. , vol.568 , pp. 178-182
    • Skrabana, R.1    Kontsek, P.2    Mederlyova, A.3    Iqbal, K.4    Novak, M.5
  • 81
    • 10844292609 scopus 로고    scopus 로고
    • Accepting its random coil nature allows a partial NMR assignment of the neuronal tau protein
    • Smet, C., Leroy, A., Sillen, A., Wieruszeski, J. M., Landrieu, I., and Lippens, G. (2004). Accepting its random coil nature allows a partial NMR assignment of the neuronal tau protein. Chembiochem 5:1639-1646.
    • (2004) Chembiochem , vol.5 , pp. 1639-1646
    • Smet, C.1    Leroy, A.2    Sillen, A.3    Wieruszeski, J.M.4    Landrieu, I.5    Lippens, G.6
  • 82
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins
    • Syme, C. D., Blanch, E. W., Holt, C., Jakes, R., Goedert, M., Hecht, L., and Barron, L. D. (2002). A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins. Eur. J. Biochem. 269:148-156.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 83
    • 0032906903 scopus 로고    scopus 로고
    • Direct effects of phosphorylation on the preferred backbone conformation of peptides: A nuclear magnetic resonance study
    • Tholey, A., Lindemann, A., Kinzel, V., and Reed, J. (1999). Direct effects of phosphorylation on the preferred backbone conformation of peptides: A nuclear magnetic resonance study. Biophys. J. 76:76-87.
    • (1999) Biophys. J. , vol.76 , pp. 76-87
    • Tholey, A.1    Lindemann, A.2    Kinzel, V.3    Reed, J.4
  • 84
    • 1642533607 scopus 로고    scopus 로고
    • The functional benefits of protein disorder
    • Tompa, P. (2003). The functional benefits of protein disorder. J. Mol. Struct.: THEOCHEM 666-667:361-371.
    • (2003) J. Mol. Struct.: THEOCHEM , vol.666-667 , pp. 361-371
    • Tompa, P.1
  • 85
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005). The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579:3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 86
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002). Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 11:739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 87
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V. N., Oldfield, C. J., and Dunker, A. K. (2005). Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18:343-384.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 88
    • 0032515086 scopus 로고    scopus 로고
    • Hyperphosphorylation induces structural modification of tau-protein
    • Uversky, V. N., Winter, S., Galzitskaya, O. V., Kittler, L., and Lober, G. (1998). Hyperphosphorylation induces structural modification of tau-protein. FEBS Lett. 439:21-25.
    • (1998) FEBS Lett. , vol.439 , pp. 21-25
    • Uversky, V.N.1    Winter, S.2    Galzitskaya, O.V.3    Kittler, L.4    Lober, G.5
  • 89
    • 0037454475 scopus 로고    scopus 로고
    • DC11: A novel monoclonal antibody revealing Alzheimer's disease-specific tau epitope
    • Vechterova, L., Kontsekova, E., Zilka, N., Ferencik, M., Ravid, R., and Novak, M. (2003). DC11: A novel monoclonal antibody revealing Alzheimer's disease-specific tau epitope. Neuroreport 14:87-91.
    • (2003) Neuroreport , vol.14 , pp. 87-91
    • Vechterova, L.1    Kontsekova, E.2    Zilka, N.3    Ferencik, M.4    Ravid, R.5    Novak, M.6
  • 91
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta 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 beta 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
  • 93
    • 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
  • 94
    • 0028826633 scopus 로고
    • Polymerization of microtubule-associated protein tau under near-physiological conditions
    • Wilson, D. M., and Binder, L. I. (1995). Polymerization of microtubule-associated protein tau under near-physiological conditions. J. Biol. Chem. 270:24306-24314.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24306-24314
    • Wilson, D.M.1    Binder, L.I.2
  • 95
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid beta 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 beta 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
  • 99
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)
    • Wood, J. G., Mirra, S. S., Pollock, N. J., and Binder, L. I. (1986). Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc. Natl. Acad. Sci. U.S.A. 83:4040-4043.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3    Binder, L.I.4
  • 100
    • 18344387559 scopus 로고    scopus 로고
    • Phosphorylation-specific prolyl isomerization: Is there an underlying theme?
    • Wulf, G., Finn, G., Suizu, F., and Lu, K. P. (2005). Phosphorylation- specific prolyl isomerization: Is there an underlying theme? Nat. Cell. Biol. 7:435-441.
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 435-441
    • Wulf, G.1    Finn, G.2    Suizu, F.3    Lu, K.P.4


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