메뉴 건너뛰기




Volumn 43, Issue 6, 2004, Pages 1694-1703

Tau Paired Helical Filaments from Alzheimer's Disease Brain and Assembled in Vitro Are Based on β-Structure in the Core Domain

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BRAIN; DISEASES; ELECTRON MICROSCOPY; IMMUNOLOGY; PURIFICATION; SOLUBILITY; SPECTROSCOPIC ANALYSIS;

EID: 1042288284     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0357006     Document Type: Article
Times cited : (196)

References (76)
  • 1
    • 0015408029 scopus 로고
    • The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation
    • Glenner, G. G., Eanes, E. D., and Page, D. L. (1972) The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation, J. Histochem. Cytochem. 20, 821-826.
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 2
    • 0037291289 scopus 로고    scopus 로고
    • Assemblies of Alzheimer's peptides Abeta25-35 and Abeta31-35: Reverse-turn conformation and side-chain interactions revealed by X-ray diffraction
    • Bond, J. P., Deverin, S. P., Inouye, H., El-Agnaf, O. M., Teeter, M. M., and Kirschner, D. A. (2003) Assemblies of Alzheimer's peptides Abeta25-35 and Abeta31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction, J. Struct. Biol. 141, 156-170.
    • (2003) J. Struct. Biol. , vol.141 , pp. 156-170
    • Bond, J.P.1    Deverin, S.P.2    Inouye, H.3    El-Agnaf, O.M.4    Teeter, M.M.5    Kirschner, D.A.6
  • 4
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling
    • Torok, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., and Langen, R. (2002) Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling, J. Biol. Chem. 277, 40810-40815.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 10
    • 0036290512 scopus 로고    scopus 로고
    • Amphipathic helical behavior of the third repeat fragment in the tau microtubule-binding domain, studied by (I)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 tau microtubule-binding domain, studied by (I)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
  • 11
    • 0033636759 scopus 로고    scopus 로고
    • The solution structure of the C-terminal segment of tau protein
    • Esposito, G., Viglino, P., Novak, M., and Cattaneo, A. (2000) The solution structure of the C-terminal segment of tau protein, J. Pept. Sci. 6, 550-559.
    • (2000) J. Pept. Sci. , vol.6 , pp. 550-559
    • Esposito, G.1    Viglino, P.2    Novak, M.3    Cattaneo, A.4
  • 12
    • 0032539585 scopus 로고    scopus 로고
    • Protein anatomy: C-tail region of human tau protein as a crucial structural element in Alzheimer's paired helical filament formation in vitro
    • Yanagawa, H., Chung, S. H., Ogawa, Y., Sato, K., Shibata-Seki, T., Masai, J., and Ishiguro, K. (1998) Protein anatomy: C-tail region of human tau protein as a crucial structural element in Alzheimer's paired helical filament formation in vitro, Biochemistry 37, 1979-1988.
    • (1998) Biochemistry , vol.37 , pp. 1979-1988
    • Yanagawa, H.1    Chung, S.H.2    Ogawa, Y.3    Sato, K.4    Shibata-Seki, T.5    Masai, J.6    Ishiguro, K.7
  • 13
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneural paired helical filaments and extraneural amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner, D. A., Abraham, C., and Selkoe, D. J. (1986) X-ray diffraction from intraneural paired helical filaments and extraneural amyloid fibers in Alzheimer disease indicates cross-β 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
  • 14
    • 0027522071 scopus 로고
    • Silver labeling of Alzheimer neurofibrillary changes and brain beta-amyloid
    • Iqbal, K., Braak, H., Braak, E., and Grundke-Iqbal, I. (1993) Silver labeling of Alzheimer neurofibrillary changes and brain beta-amyloid, J. Histotechnol. 16, 335-342.
    • (1993) J. Histotechnol. , vol.16 , pp. 335-342
    • Iqbal, K.1    Braak, H.2    Braak, E.3    Grundke-Iqbal, I.4
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Perez, M., Valpuesta, J. M., Medina, M., Montejo de Garcini, E., and Avila, J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction, J. Neurochem. 67, 1183-1190.
    • (1996) J. Neurochem. , vol.67 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 18
    • 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., and Mandelkow, E. M. (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
  • 19
    • 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
  • 20
    • 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., 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.6
  • 22
    • 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
  • 23
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-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 beta-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
  • 24
    • 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
  • 25
    • 0033677809 scopus 로고    scopus 로고
    • C-Terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V., Berry, R. W., Kuret, J., and Binder, L. I. (2000) C-Terminal inhibition of tau assembly in vitro and in Alzheimer's disease, J. Cell Sci. 113 (Part 21), 3737-3745.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 21 , pp. 3737-3745
    • Abraha, A.1    Ghoshal, N.2    Gamblin, T.C.3    Cryns, V.4    Berry, R.W.5    Kuret, J.6    Binder, L.I.7
  • 26
    • 0034494233 scopus 로고    scopus 로고
    • Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: Implications for the formation of paired helical filaments
    • Giannetti, A. M., Lindwall, G., Chau, M. F., Radeke, M. J., Feinstein, S. C., and Kohlstaedt, L. A. (2000) Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments, Protein Sci. 9, 2427-2435.
    • (2000) Protein Sci. , vol.9 , pp. 2427-2435
    • Giannetti, A.M.1    Lindwall, G.2    Chau, M.F.3    Radeke, M.J.4    Feinstein, S.C.5    Kohlstaedt, L.A.6
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0032951956 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of recombinant tau by the paired-helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase
    • Jicha, G. A., O'Donnell, A., Weaver, C., Angeletti, R., and Davies, P. (1999) Hierarchical phosphorylation of recombinant tau by the paired-helical filament-associated protein kinase is dependent on cyclic AMP-dependent protein kinase, J. Neurochem. 72, 214-224.
    • (1999) J. Neurochem. , vol.72 , pp. 214-224
    • Jicha, G.A.1    O'Donnell, A.2    Weaver, C.3    Angeletti, R.4    Davies, P.5
  • 31
    • 0026521716 scopus 로고
    • A protein kinase associated with paired helical filaments in Alzheimer disease
    • Vincent, I. J., and Davies, P. (1992) A protein kinase associated with paired helical filaments in Alzheimer disease, Proc. Natl. Acad. Sci. U.S.A. 89, 2878-2882.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2878-2882
    • Vincent, I.J.1    Davies, P.2
  • 32
    • 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
  • 34
    • 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., Crowther, R., Walker, J., 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.2    Crowther, R.3    Walker, J.4    Klug, A.5
  • 36
    • 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
  • 37
    • 0344043346 scopus 로고    scopus 로고
    • Protein structure prediction. Implications for the biologist
    • Deleage, G., Blanchet, C., and Geourjon, C. (1997) Protein structure prediction. Implications for the biologist, Biochimie 79, 681-686.,
    • (1997) Biochimie , vol.79 , pp. 681-686
    • Deleage, G.1    Blanchet, C.2    Geourjon, C.3
  • 38
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 39
    • 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
  • 40
    • 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
  • 41
    • 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
    • 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 Jr., L.3    Trojanowski, J.Q.4
  • 44
    • 0025949088 scopus 로고
    • A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities
    • Brion, J. P., Hanger, D. P., Couck, A. M., and Anderton, B. H. (1991) A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities, Biochem. J. 279 (Part 3), 831-836.
    • (1991) Biochem. J. , vol.279 , Issue.PART 3 , pp. 831-836
    • Brion, J.P.1    Hanger, D.P.2    Couck, A.M.3    Anderton, B.H.4
  • 45
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, G., Cairns, N. J., and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms, Neuron 8, 159-168.
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, G.2    Cairns, N.J.3    Crowther, R.A.4
  • 46
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 48
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. (1995) Circular dichroism, Methods Enzymol. 246, 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 49
    • 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
  • 50
    • 0035882542 scopus 로고    scopus 로고
    • Denatured collapsed states in protein folding: Example of apomyoglobin
    • Tcherkasskaya, O., and Uversky, V. N. (2001) Denatured collapsed states in protein folding: example of apomyoglobin, Proteins 44, 244-254.
    • (2001) Proteins , vol.44 , pp. 244-254
    • Tcherkasskaya, O.1    Uversky, V.N.2
  • 51
    • 0021113184 scopus 로고
    • Molecular flexibility in microtubule proteins: Proton nuclear magnetic resonance characterization
    • Woody, R. W., Clark, D. C., Roberts, G. C., Martin, S. R., and Bayley, P. M. (1983) Molecular flexibility in microtubule proteins: proton nuclear magnetic resonance characterization, Biochemistry 22, 2186-2192.
    • (1983) Biochemistry , vol.22 , pp. 2186-2192
    • Woody, R.W.1    Clark, D.C.2    Roberts, G.C.3    Martin, S.R.4    Bayley, P.M.5
  • 53
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., Yang, J. T., and Chau, K. H. (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism, Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 54
    • 0028820601 scopus 로고
    • Analysis of i,i+5 and i,i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif
    • Munoz, V., and Serrano, L. (1995) Analysis of i,i+5 and i,i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif, Biochemistry 34, 15301-15306.
    • (1995) Biochemistry , vol.34 , pp. 15301-15306
    • Munoz, V.1    Serrano, L.2
  • 55
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 56
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert, F. (1995) Infrared spectroscopy applied to biochemical and biological problems, Methods Enzymol. 246, 501-526.
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 57
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi, H., and Byler, D. M. (1986) Resolution-enhanced Fourier transform infrared spectroscopy of enzymes, Methods Enzymol. 130, 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 58
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H., and Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment, Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 59
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide
    • Permanne, B., Adessi, C., Saborio, G. P., Fraga, S., Frossard, M. J., Van Dorpe, J., Dewachter, I., Banks, W. A., Van Leuven, F., and Soto, C. (2002) Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide, FASEB J. 16, 860-862.
    • (2002) FASEB J. , vol.16 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3    Fraga, S.4    Frossard, M.J.5    Van Dorpe, J.6    Dewachter, I.7    Banks, W.A.8    Van Leuven, F.9    Soto, C.10
  • 60
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. (2002) A possible role for pi-stacking in the self-assembly of amyloid fibrils, FASEB J. 16, 77-83.
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 61
    • 0036931473 scopus 로고    scopus 로고
    • Neurofibrillary degeneration can be arrested in an in vivo cellular model of human tauopathy by application of a compound which inhibits tau filament formation in vitro
    • Hall, G. F., Lee, S., and Yao, J. (2002) Neurofibrillary degeneration can be arrested in an in vivo cellular model of human tauopathy by application of a compound which inhibits tau filament formation in vitro, J. Mol. Neurosci. 19, 253-260.
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 253-260
    • Hall, G.F.1    Lee, S.2    Yao, J.3
  • 63
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson, G. R., Wiedau-Pazos, M., Sang, T. K., Wagle, N., Brown, C. A., Massachi, S., and Geschwind, D. H. (2002) Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila, Neuron. 34, 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 65
    • 0036927254 scopus 로고    scopus 로고
    • Discovery of compounds that will prevent tau pathology
    • Kosik, K. S., Ahn, J., Stein, R., and Yeh, L. A. (2002) Discovery of compounds that will prevent tau pathology, J. Mol. Neurosci. 19, 261-266.
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 261-266
    • Kosik, K.S.1    Ahn, J.2    Stein, R.3    Yeh, L.A.4
  • 66
    • 0029002914 scopus 로고
    • Analysis of the core components of Alzheimer paired helical filaments. A gas chromatography/mass spectrometry characterization of fatty acids, carbohydrates and long-chain bases
    • Goux, W. J., Rodriguez, S., and Sparkman, D. R. (1995) Analysis of the core components of Alzheimer paired helical filaments. A gas chromatography/ mass spectrometry characterization of fatty acids, carbohydrates and long-chain bases, FEBS Lett. 366, 81-85.
    • (1995) FEBS Lett. , vol.366 , pp. 81-85
    • Goux, W.J.1    Rodriguez, S.2    Sparkman, D.R.3
  • 67
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N., and Woody, R. W. (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism, Anal. Biochem. 209, 32-44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 69
    • 0034630136 scopus 로고    scopus 로고
    • Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy
    • Baello, B. I., Pancoska, P., and Keiderling, T. A. (2000) Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy, Anal. Biochem. 280, 46-57.
    • (2000) Anal. Biochem. , vol.280 , pp. 46-57
    • Baello, B.I.1    Pancoska, P.2    Keiderling, T.A.3
  • 71
    • 0041630890 scopus 로고    scopus 로고
    • Structure and texture of fibrous crystals formed by Alzheimer's abeta(11-25) peptide fragment
    • Sikorski, P., Atkins, E. D., and Serpell, L. C. (2003) Structure and texture of fibrous crystals formed by Alzheimer's abeta(11-25) peptide fragment, Structure 11, 915-926.
    • (2003) Structure , vol.11 , pp. 915-926
    • Sikorski, P.1    Atkins, E.D.2    Serpell, L.C.3
  • 72
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis, Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 73
    • 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
  • 74
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra, F., Ghoshal, N., Quinn, B., Berry, R. W., and Binder, L. I. (2003) Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease, J. Alzheimer's Dis. 5, 65-77.
    • (2003) J. Alzheimer's Dis. , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1    Ghoshal, N.2    Quinn, B.3    Berry, R.W.4    Binder, L.I.5
  • 75
    • 0022457104 scopus 로고
    • A neuronal antigen in the brains of Alzheimer patients
    • Wolozin, B. L., Pruchnicki, A., Dickson, D. W., and Davies, P. (1986) A neuronal antigen in the brains of Alzheimer patients, Science 232, 648-650.
    • (1986) Science , vol.232 , pp. 648-650
    • Wolozin, B.L.1    Pruchnicki, A.2    Dickson, D.W.3    Davies, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.