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Volumn 45, Issue 7, 2006, Pages 2283-2293

Global hairpin folding of tau in solution

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; ELECTRON MOBILITY; ENERGY TRANSFER; MUTAGENESIS; PARAMAGNETIC RESONANCE; PROXIMITY INDICATORS;

EID: 33144463940     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0521543     Document Type: Article
Times cited : (347)

References (67)
  • 1
    • 0035140975 scopus 로고    scopus 로고
    • Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease
    • Garcia, M. L., and Cleveland, D. W. (2001) Going new places using an old MAP: Tau, microtubules and human neurodegenerative disease, Curr. Opin. Cell Biol. 13, 41-8.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 41-48
    • Garcia, M.L.1    Cleveland, D.W.2
  • 2
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003) Modeling tau polymerization in vitro: A review and synthesis, Biochemistry 42, 15009-17.
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 4
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland, D. W., Hwo, S. Y., and Kirschner, M. W. (1977) Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly, J. Mol. Biol. 116, 227-47.
    • (1977) J. Mol. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 5
    • 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, 573-84.
    • (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
  • 6
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure
    • Schweers, O., Schonbrunn-Hanebeck, E., Marx, A., and Mandelkow, E. (1994) Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure, J. Biol. Chem. 269, 24290-7.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 7
    • 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, 5129-34.
    • (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
  • 8
    • 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, 14885-96.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 9
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen, J., Kanai, Y., Cowan, N. J., and Hirokawa, N. (1992) Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons, Nature 360, 674-7.
    • (1992) Nature , vol.360 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 10
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K. A., and Kirschner, M. W. (1991) Tau protein binds to microtubules through a flexible array of distributed weak sites, J. Cell Biol. 115, 717-30.
    • (1991) J. Cell Biol. , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 12
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • Goode, B. L., Denis, P. E., Panda, D., Radeke, M. J., Miller, H. P., Wilson, L., and Feinstein, S. C. (1997) Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly, Mol. Biol. Cell 8, 353-65.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 353-365
    • Goode, B.L.1    Denis, P.E.2    Panda, D.3    Radeke, M.J.4    Miller, H.P.5    Wilson, L.6    Feinstein, S.C.7
  • 13
    • 17144409371 scopus 로고    scopus 로고
    • Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegeneration
    • Levy, S. F., Leboeuf, A. C., Massie, M. R., Jordan, M. A., Wilson, L., and Feinstein, S. C. (2005) Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegeneration, J. Biol. Chem. 280, 13520-8.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13520-13528
    • Levy, S.F.1    Leboeuf, A.C.2    Massie, M.R.3    Jordan, M.A.4    Wilson, L.5    Feinstein, S.C.6
  • 15
    • 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, 2725-9.
    • (1991) EMBO J. , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 16
    • 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, 10223-30.
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 17
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure
    • von Bergen, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2001) Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-structure, J. Biol. Chem. 276, 48165-74.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 18
    • 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, 1694-703.
    • (2004) Biochemistry , vol.43 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 19
    • 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, 365-70.
    • (1993) EMBO J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 22
    • 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, 550-3.
    • (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
  • 23
    • 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, 344-9.
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 24
    • 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), 3737-45.
    • (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
  • 27
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's ammo-terminal projection domain
    • Brandt, R., Leger, J., and Lee, G. (1995) Interaction of tau with the neural plasma membrane mediated by tau's ammo-terminal projection domain, J. Cell Biol. 131, 1327-40.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 28
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies
    • Sontag, E., Nunbhakdi-Craig, V., Lee, G., Brandt, R., Kamibayashi, C., Kuret, J., White, C. L., III, Mumby, M. C., and Bloom, G. S. (1999) Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies, J. Biol. Chem. 274, 25490-8.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6    White III, C.L.7    Mumby, M.C.8    Bloom, G.S.9
  • 30
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003) Tau polymerization: Role of the amino terminus, Biochemistry 42, 2252-7.
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 31
    • 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, 128-32.
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 32
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal-antibody Alz50s selectivity for Alzheimer's-disease pathology
    • Carmel, G., Mager, E. M., Binder, L. I., and Kuret, J. (1996) The structural basis of monoclonal-antibody Alz50s selectivity for Alzheimer's-disease pathology, J. Biol. Chem. 271, 32789-95.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 33
    • 0026551711 scopus 로고
    • The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region
    • Biernat, J., Mandelkow, E. M., Schroter, C., Lichtenberg-Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., Goedert, M., et al. (1992) The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region, EMBO J. 11, 1593-7.
    • (1992) EMBO J. , vol.11 , pp. 1593-1597
    • Biernat, J.1    Mandelkow, E.M.2    Schroter, C.3    Lichtenberg-Kraag, B.4    Steiner, B.5    Berling, B.6    Meyer, H.7    Mercken, M.8    Vandermeeren, A.9    Goedert, M.10
  • 34
    • 0015820465 scopus 로고
    • Synthesis and characterization of two fluorescent sulfhydryl reagents
    • Hudson, E. N., and Weber, G. (1973) Synthesis and characterization of two fluorescent sulfhydryl reagents, Biochemistry 12, 4154-61.
    • (1973) Biochemistry , vol.12 , pp. 4154-4161
    • Hudson, E.N.1    Weber, G.2
  • 36
    • 0027931587 scopus 로고
    • Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements
    • Wu, P., and Brand, L. (1994) Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements, Biochemistry 33, 10457-62.
    • (1994) Biochemistry , vol.33 , pp. 10457-10462
    • Wu, P.1    Brand, L.2
  • 37
    • 0016429773 scopus 로고
    • Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase
    • Matsumoto, S., and Hammes, G. G. (1975) Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase, Biochemistry 14, 214-24.
    • (1975) Biochemistry , vol.14 , pp. 214-224
    • Matsumoto, S.1    Hammes, G.G.2
  • 38
    • 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, 12497-502.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12497-12502
    • Fitzkee, N.C.1    Rose, G.D.2
  • 39
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., and Crowther, R. A. (1989) Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain, EMBO J. 8, 393-9.
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 40
    • 0036830506 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
    • Li, L., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2002) Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis, J. Biol. Chem. 277, 41390-400.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 42
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M. R. (1991) Fluorescence techniques for studying protein structure, Methods Biochem. Anal. 35, 127-205.
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 43
    • 3142735737 scopus 로고    scopus 로고
    • Methods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy
    • Steinhoff, H. J. (2002) Methods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy, Front Biosci. 7, c97-110.
    • (2002) Front Biosci. , vol.7
    • Steinhoff, H.J.1
  • 44
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling, Nat. Struct. Biol. 7, 735-9.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 45
    • 0022033590 scopus 로고
    • Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH: Acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • Lund, J., and Dalton, H. (1985) Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH: acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath), Eur. J. Biochem. 147, 291-6.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 291-296
    • Lund, J.1    Dalton, H.2
  • 46
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai, M., and Langen, R. (2004) Template-assisted filament growth by parallel stacking of tau, Proc. Natl Acad. Sci. U.S.A. 101, 10278-83.
    • (2004) Proc. Natl Acad. Sci. U.S.A. , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 47
    • 0025194961 scopus 로고
    • Residual motion of hemoglobin-bound spin labels and protein dynamics: Viscosity dependence of the rotational correlation times
    • Steinhoff, H. J. (1990) Residual motion of hemoglobin-bound spin labels and protein dynamics: Viscosity dependence of the rotational correlation times, Eur. Biophys. J. 18, 57-62.
    • (1990) Eur. Biophys. J. , vol.18 , pp. 57-62
    • Steinhoff, H.J.1
  • 48
    • 0038581168 scopus 로고    scopus 로고
    • Polymeric aspects of protein folding: A brief overview
    • Tcherkasskaya, O., and Uversky, V. N. (2003) Polymeric aspects of protein folding: A brief overview, Protein Pept. Lett. 10, 239-45.
    • (2003) Protein Pept. Lett. , vol.10 , pp. 239-245
    • Tcherkasskaya, O.1    Uversky, V.N.2
  • 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, 739-56.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 51
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., and Milligan, R. A. (2002) MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments, J. Cell Biol. 157, 1187-96.
    • (2002) J. Cell Biol. , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 55
    • 0842265772 scopus 로고    scopus 로고
    • Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain
    • Minoura, K., Yao, T. M., Tomoo, K., Sumida, M., Sasaki, M., Taniguchi, T., and Ishida, T. (2004) Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain, Eur. J. Biochem. 271, 545-52.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 545-552
    • Minoura, K.1    Yao, T.M.2    Tomoo, K.3    Sumida, M.4    Sasaki, M.5    Taniguchi, T.6    Ishida, T.7
  • 56
    • 10944258455 scopus 로고    scopus 로고
    • Tau aggregation is driven by a transition from random coil to β sheet structure
    • von Bergen, M., Barghorn, S., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2005) Tau aggregation is driven by a transition from random coil to β sheet structure, Biochim. Biophys. Acta 1739, 158-66.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 158-166
    • Bergen, M.1    Barghorn, S.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 57
    • 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, 2087-95.
    • (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
  • 59
    • 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
  • 60
    • 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. (2004) Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423, FEBS Lett. 568, 178-82.
    • (2004) FEBS Lett. , vol.568 , pp. 178-182
    • Skrabana, R.1    Kontsek, P.2    Mederlyova, A.3    Iqbal, K.4    Novak, M.5
  • 62
    • 0034971707 scopus 로고    scopus 로고
    • Missense and splice site mutations in tau associated with FTDP-17: Multiple pathogenic mechanisms
    • Hutton, M. (2001) Missense and splice site mutations in tau associated with FTDP-17: Multiple pathogenic mechanisms, Neurology 56, S21-5.
    • (2001) Neurology , vol.56
    • Hutton, M.1
  • 63
    • 0037016024 scopus 로고    scopus 로고
    • Formation of the hydrophobic core of ribonuclease a through sequential coordinated conformational transitions
    • Navon, A., Ittah, V., Scheraga, H. A., and Haas, E. (2002) Formation of the hydrophobic core of ribonuclease A through sequential coordinated conformational transitions, Biochemistry 41, 14225-31.
    • (2002) Biochemistry , vol.41 , pp. 14225-14231
    • Navon, A.1    Ittah, V.2    Scheraga, H.A.3    Haas, E.4
  • 64
    • 7944221639 scopus 로고    scopus 로고
    • Acid-induced unfolding of the aminoterminal domains of the lethal and edema factors of anthrax toxin
    • Krantz, B. A., Trivedi, A. D., Cunningham, K., Christensen, K. A., and Collier, R. J. (2004) Acid-induced unfolding of the aminoterminal domains of the lethal and edema factors of anthrax toxin, J. Mol. Biol. 344, 739-56.
    • (2004) J. Mol. Biol. , vol.344 , pp. 739-756
    • Krantz, B.A.1    Trivedi, A.D.2    Cunningham, K.3    Christensen, K.A.4    Collier, R.J.5
  • 65
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler, B., Lipman, E. A., and Eaton, W. A. (2002) Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy, Nature 419, 743-7.
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.