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Volumn 44, Issue 1, 2005, Pages 149-156

Role for the α-helix in aberrant protein aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; DISEASE CONTROL; MORPHOLOGY; NEUROLOGY; SPECTROSCOPIC ANALYSIS;

EID: 11844262626     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048564t     Document Type: Article
Times cited : (49)

References (40)
  • 1
    • 0001444341 scopus 로고
    • Configuration of Polypeptide Chains
    • Pauling, L., and Corey, R. B. (1951) Configuration of Polypeptide Chains, Nature 168, 550-551.
    • (1951) Nature , vol.168 , pp. 550-551
    • Pauling, L.1    Corey, R.B.2
  • 3
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism
    • Parry, D. A. D., and Steinert, P. M. (1999) Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism, Q. Rev. Biophys. 32, 99-187.
    • (1999) Q. Rev. Biophys. , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 4
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P., Pepys, C., and Blake, C. C. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction, J. Mol. Biol. 273, 729-739.
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.4    Pepys, C.5    Blake, C.C.6
  • 5
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • Sunde, M., and Blake, C. C. (1998) From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation, Q. Rev. Biophys. 31, 1039.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 1039
    • Sunde, M.1    Blake, C.C.2
  • 6
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding. Nature 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 7
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin, Nature 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 8
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/ water mixtures back to water
    • Luo, P. Z., and Baldwin, R. L. (1997) Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water, Biochemistry 36, 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.Z.1    Baldwin, R.L.2
  • 9
    • 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
  • 10
    • 0142139311 scopus 로고    scopus 로고
    • Tau protein in familial and sporadic diseases
    • Yancopoulou, D., and Spillantini, M. G. (2003) Tau protein in familial and sporadic diseases, Neuromol. Med. 4, 37-48.
    • (2003) Neuromol. Med. , vol.4 , pp. 37-48
    • Yancopoulou, D.1    Spillantini, M.G.2
  • 12
    • 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
  • 13
    • 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
  • 17
    • 0032516190 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G., and Downing, K. H. (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature 393, 191.
    • (1998) Nature , vol.393 , pp. 191
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 18
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure
    • Berriman, J., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., and Crowther, R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-β structure, Proc. Natl. Acad. Sci. U.S.A. 100, 9034-9038.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9034-9038
    • Berriman, J.1    Serpell, L.C.2    Oberg, K.A.3    Fink, A.L.4    Goedert, M.5    Crowther, R.A.6
  • 19
    • 0028301327 scopus 로고
    • NMR Solution Structure of the Isolated N-Terminal Fragment of Protein-G B-1 Domain: Evidence of Trifluoroethanol Induced Native-Like β-Hairpin Formation
    • Blanco, F. J., Jimenez, M. A., Pineda, A., Rico, M., Santoro, J., and Nieto, J. L. (1994) NMR Solution Structure of the Isolated N-Terminal Fragment of Protein-G B-1 Domain: Evidence of Trifluoroethanol Induced Native-Like β-Hairpin Formation. Biochemistry 33, 6004-6014.
    • (1994) Biochemistry , vol.33 , pp. 6004-6014
    • Blanco, F.J.1    Jimenez, M.A.2    Pineda, A.3    Rico, M.4    Santoro, J.5    Nieto, J.L.6
  • 20
    • 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, 15009-15017.
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 21
    • 0345827608 scopus 로고    scopus 로고
    • Sequence determinants of amyloid fibril formation
    • de la Paz, M. L., and Serrano, L. (2004) Sequence determinants of amyloid fibril formation, Proc. Natl. Acad. Sci. U.S.A. 101, 87-92.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 87-92
    • De La Paz, M.L.1    Serrano, L.2
  • 23
    • 0342368837 scopus 로고    scopus 로고
    • The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules
    • Perez, M., Lim, F., Arrasate, M., and Avila, J. (2000) The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules, J. Neurochem. 74, 2583-2589.
    • (2000) J. Neurochem. , vol.74 , pp. 2583-2589
    • Perez, M.1    Lim, F.2    Arrasate, M.3    Avila, J.4
  • 24
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry, E. R., and Hofrichter, J. (1992) Singular value decomposition: Application to analysis of experimental data, Methods Enzymol. 210, 129-192.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 25
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Muñoz, V., and Serrano, L. (1994) Elucidating the folding problem of helical peptides using empirical parameters, Nat. Struct. Biol. 1, 399-409.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Muñoz, V.1    Serrano, L.2
  • 26
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz, V., and Serrano, L. (1997) Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms, Biopolymers 41, 495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 27
    • 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
    • 11844252233 scopus 로고    scopus 로고
    • American Chemical Society, Washington, DC
    • Singh, B. R. (2000) in ACS Symposium Series, American Chemical Society, Washington, DC.
    • (2000) ACS Symposium Series
    • Singh, B.R.1
  • 30
    • 0030019825 scopus 로고    scopus 로고
    • Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins
    • Heimburg, T., Schuenemann, J., Weber, K., and Geisler, N. (1996) Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins, Biochemistry 35, 1375-1382.
    • (1996) Biochemistry , vol.35 , pp. 1375-1382
    • Heimburg, T.1    Schuenemann, J.2    Weber, K.3    Geisler, N.4
  • 31
    • 0016169865 scopus 로고
    • Determination of the helix and β 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 β 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
  • 32
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimers 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 Alzheimers 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
  • 33
    • 0037291995 scopus 로고    scopus 로고
    • The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils
    • Bousset, L., Briki, F., Doucet, J., and Melki, R. (2003) The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils, J. Struct. Biol. 141, 132-142.
    • (2003) J. Struct. Biol. , vol.141 , pp. 132-142
    • Bousset, L.1    Briki, F.2    Doucet, J.3    Melki, R.4
  • 34
    • 0000236570 scopus 로고
    • Peptide Velcro: Design of a Heterodimeric Coiled-Coil
    • Oshea, E. K., Lumb, K. J., and Kim, P. S. (1993) Peptide Velcro: Design of a Heterodimeric Coiled-Coil, Curr. Biol. 3, 658-667.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • Oshea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 35
    • 0026356891 scopus 로고
    • Predicting Coiled Coils from Protein Sequences
    • Lupas, A., Vandyke, M., and Stock, J. (1991) Predicting Coiled Coils from Protein Sequences, Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Vandyke, M.2    Stock, J.3
  • 37
    • 0037065734 scopus 로고    scopus 로고
    • Effect of phosphorylation on α-helix stability as a function of position
    • Andrew, C. D., Warwicker, J., Jones, G. R., and Doig, A. J. (2002) Effect of phosphorylation on α-helix stability as a function of position, Biochemistry 41, 1897-1905.
    • (2002) Biochemistry , vol.41 , pp. 1897-1905
    • Andrew, C.D.1    Warwicker, J.2    Jones, G.R.3    Doig, A.J.4
  • 38
    • 0347653719 scopus 로고    scopus 로고
    • Bending rigidity of stiff polyelectrolyte chains: A single chain and a bundle of multichains
    • Ha, B. Y., and Thirumalai, D. (2003) Bending rigidity of stiff polyelectrolyte chains: A single chain and a bundle of multichains, Macromolecules 36, 9658-9666.
    • (2003) Macromolecules , vol.36 , pp. 9658-9666
    • Ha, B.Y.1    Thirumalai, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.