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Volumn 447, Issue 1, 2012, Pages 43-50

Structural origin of polymorphism of Alzheimer's amyloid β-fibrils

Author keywords

sheet twist; Amyloid peptide (A ); Electron paramagnetic resonance (EPR); Spin labelling

Indexed keywords

AMYLOID BETA PROTEIN[1-40];

EID: 84866389512     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120034     Document Type: Article
Times cited : (30)

References (53)
  • 1
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: Conformational diversity and consequences
    • Toyama, B. H. and Weissman, J. S. (2011) Amyloid structure: conformational diversity and consequences. Annu. Rev. Biochem. 80, 557-585
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 2
    • 79956323218 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity
    • Lee, Y. J., Savtchenko, R., Ostapchenko, V. G., Makarava, N. and Baskakov, I. V. (2011) Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity. PLoS ONE 6, e20244
    • (2011) PLoS ONE , vol.6
    • Lee, Y.J.1    Savtchenko, R.2    Ostapchenko, V.G.3    Makarava, N.4    Baskakov, I.V.5
  • 3
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., Leapman, R. D., Guo, Z. H., Yau, W. M., Mattson, M. P. and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307, 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.H.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 4
    • 77955273305 scopus 로고    scopus 로고
    • Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated
    • Kodali, R., Williams, A. D., Chemuru, S. and Wetzel, R. (2010) Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated. J. Mol. Biol. 401, 503-517
    • (2010) J. Mol. Biol. , vol.401 , pp. 503-517
    • Kodali, R.1    Williams, A.D.2    Chemuru, S.3    Wetzel, R.4
  • 5
    • 59649110455 scopus 로고    scopus 로고
    • Aβ(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
    • Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N. and Fandrich, M. (2009) Aβ(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J. Mol. Biol. 386, 869-877
    • (2009) J. Mol. Biol. , vol.386 , pp. 869-877
    • Meinhardt, J.1    Sachse, C.2    Hortschansky, P.3    Grigorieff, N.4    Fandrich, M.5
  • 6
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • Paravastu, A. K., Qahwash, I., Leapman, R. D., Meredith, S. C. and Tycko, R. (2009) Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc. Natl. Acad. Sci. U.S.A. 106, 7443-7448
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 7
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko, R. (2011) Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem. 62, 279-299
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 279-299
    • Tycko, R.1
  • 8
    • 0015914783 scopus 로고
    • Conformation of twisted β-pleated sheets in proteins
    • Chothia, C. (1973) Conformation of twisted β-pleated sheets in proteins. J. Mol. Biol. 75, 295-302
    • (1973) J. Mol. Biol. , vol.75 , pp. 295-302
    • Chothia, C.1
  • 9
    • 0000573263 scopus 로고
    • Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets
    • Pauling, L. and Corey, R. B. (1951) Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets. Proc. Natl. Acad. Sci. U.S.A. 37, 729-740
    • (1951) Proc. Natl. Acad. Sci. U.S.A. , vol.37 , pp. 729-740
    • Pauling, L.1    Corey, R.B.2
  • 10
    • 0020491376 scopus 로고
    • Structure of β-sheets - Origin of the right-handed twist and of the increased stability of antiparallel over parallel sheets
    • Chou, K. C., Pottle, M., Nemethy, G., Ueda, Y. and Scheraga, H. A. (1982) Structure of β-sheets - origin of the right-handed twist and of the increased stability of antiparallel over parallel sheets. J. Mol. Biol. 162, 89-112
    • (1982) J. Mol. Biol. , vol.162 , pp. 89-112
    • Chou, K.C.1    Pottle, M.2    Nemethy, G.3    Ueda, Y.4    Scheraga, H.A.5
  • 11
    • 0001244377 scopus 로고
    • Origin of the right-handed twist of β-sheets of poly(L-Val) chains
    • Chou, K. C. and Scheraga, H. A. (1982) Origin of the right-handed twist of β-sheets of poly(L-Val) chains. Proc. Natl. Acad. Sci. U.S.A. 79, 7047-7051
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 7047-7051
    • Chou, K.C.1    Scheraga, H.A.2
  • 12
    • 0021095536 scopus 로고
    • Role of interchain interactions in the stabilization of the right-handed twist of β-sheets
    • Chou, K. C., Nemethy, G. and Scheraga, H. A. (1983) Role of interchain interactions in the stabilization of the right-handed twist of β-sheets. J. Mol. Biol. 168, 389-407
    • (1983) J. Mol. Biol. , vol.168 , pp. 389-407
    • Chou, K.C.1    Nemethy, G.2    Scheraga, H.A.3
  • 13
    • 0020991935 scopus 로고
    • Structural properties of protein β-sheets
    • Salemme, F. R. (1983) Structural properties of protein β-sheets. Prog. Biophys. Mol. Biol. 42, 95-133
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 95-133
    • Salemme, F.R.1
  • 14
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling
    • Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G. and Langen, R. (2002) Structural and dynamic features of Alzheimer's Aβ 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
    • Török, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 15
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., Yau, W. M. and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45, 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 16
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu, A. K., Leapman, R. D., Yau, W. M. and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 105, 18349-18354
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 18
    • 34250206336 scopus 로고    scopus 로고
    • Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides
    • Shahnawaz, M., Thapa, A. and Park, I. S. (2007) Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides. Biochem. Biophys. Res. Commun. 359, 801-805
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 801-805
    • Shahnawaz, M.1    Thapa, A.2    Park, I.S.3
  • 19
    • 80054942374 scopus 로고    scopus 로고
    • Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease
    • Ngo, S. and Guo, Z. (2011) Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease. Biochem. Biophys. Res. Commun. 414, 512-516
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 512-516
    • Ngo, S.1    Guo, Z.2
  • 20
    • 84858612961 scopus 로고    scopus 로고
    • Solid-support EPR studies of Aβ40 monomers reveal a structured state with three ordered segments
    • Gu, L., Ngo, S. and Guo, Z. (2012) Solid-support EPR studies of Aβ40 monomers reveal a structured state with three ordered segments. J. Biol. Chem. 287, 9081-9089
    • (2012) J. Biol. Chem. , vol.287 , pp. 9081-9089
    • Gu, L.1    Ngo, S.2    Guo, Z.3
  • 21
    • 79952144525 scopus 로고    scopus 로고
    • High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins
    • McCoy, J. and Hubbell, W. L. (2011) High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins. Proc. Natl. Acad. Sci. U.S.A. 108, 1331-1336
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 1331-1336
    • McCoy, J.1    Hubbell, W.L.2
  • 22
    • 0001867405 scopus 로고
    • Calculating slow motional magnetic resonance specta
    • Berliner, L. J. and Reuben, J., eds, Plenum Press, New York
    • Schneider, D. J. and Freed, J. H. (1989) Calculating slow motional magnetic resonance specta. In Spin Labeling: Theory and Applications (Berliner, L. J. and Reuben, J., eds), pp. 1-76, Plenum Press, New York
    • (1989) Spin Labeling: Theory and Applications , pp. 1-76
    • Schneider, D.J.1    Freed, J.H.2
  • 23
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm
    • Budil, D. E., Lee, S., Saxena, S. and Freed, J. H. (1996) Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J. Magn. Reson. 120, 155-189
    • (1996) J. Magn. Reson. , vol.120 , pp. 155-189
    • Budil, D.E.1    Lee, S.2    Saxena, S.3    Freed, J.H.4
  • 24
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • Columbus, L., Kálai, T., Jeko, J., Hideg, K. and Hubbell, W. L. (2001) Molecular motion of spin labeled side chains in α-helices: analysis by variation of side chain structure. Biochemistry 40, 3828-3846
    • (2001) Biochemistry , vol.40 , pp. 3828-3846
    • Columbus, L.1    Kálai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 25
    • 34249794011 scopus 로고    scopus 로고
    • Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme
    • Guo, Z., Cascio, D., Hideg, K., Kálai, T. and Hubbell, W. L. (2007) Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme. Protein Sci. 16, 1069-1086
    • (2007) Protein Sci. , vol.16 , pp. 1069-1086
    • Guo, Z.1    Cascio, D.2    Hideg, K.3    Kálai, T.4    Hubbell, W.L.5
  • 26
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • Altenbach, C., Oh, K. J., Trabanino, R. J., Hideg, K. and Hubbell, W. L. (2001) Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. Biochemistry 40, 15471-15482
    • (2001) Biochemistry , vol.40 , pp. 15471-15482
    • Altenbach, C.1    Oh, K.J.2    Trabanino, R.J.3    Hideg, K.4    Hubbell, W.L.5
  • 27
    • 57649128935 scopus 로고    scopus 로고
    • Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: Molecular insights from electron paramagnetic resonance spectroscopy
    • Margittai, M. and Langen, R. (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Q. Rev. Biophys. 41, 265-297
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 265-297
    • Margittai, M.1    Langen, R.2
  • 32
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. (2006) Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 39, 1-55
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 34
    • 0036296028 scopus 로고    scopus 로고
    • Twist and shear in &beta-sheets and β-ribbons
    • Ho, B. K. and Curmi, P. M. G. (2002) Twist and shear in &beta-sheets and β-ribbons. J. Mol. Biol. 317, 291-308
    • (2002) J. Mol. Biol. , vol.317 , pp. 291-308
    • Ho, B.K.1    Curmi, P.M.G.2
  • 37
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-β fibril polymorphisms
    • Goldsbury, C., Frey, P., Olivieri, V., Aebi, U. and Muller, S. A. (2005) Multiple assembly pathways underlie amyloid-β fibril polymorphisms. J. Mol. Biol. 352, 282-298
    • (2005) J. Mol. Biol. , vol.352 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Muller, S.A.5
  • 38
  • 41
    • 79251539305 scopus 로고    scopus 로고
    • Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers
    • Pifer, P. M., Yates, E. A. and Legleiter, J. (2011) Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers. PLoS ONE 6, e16248
    • (2011) PLoS ONE , vol.6
    • Pifer, P.M.1    Yates, E.A.2    Legleiter, J.3
  • 43
  • 45
    • 79958058969 scopus 로고    scopus 로고
    • Recent progress in understanding Alzheimer's β-amyloid structures
    • Fandrich, M., Schmidt, M. and Grigorieff, N. (2011) Recent progress in understanding Alzheimer's β-amyloid structures. Trends Biochem. Sci. 36, 338-345
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 338-345
    • Fandrich, M.1    Schmidt, M.2    Grigorieff, N.3
  • 46
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali, R. and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol. 17, 48-57
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 47
    • 80051934831 scopus 로고    scopus 로고
    • Hierarchical organization in the amyloid core of yeast prion protein Ure2
    • Ngo, S., Gu, L. and Guo, Z. (2011) Hierarchical organization in the amyloid core of yeast prion protein Ure2. J. Biol. Chem. 286, 29691-29699
    • (2011) J. Biol. Chem. , vol.286 , pp. 29691-29699
    • Ngo, S.1    Gu, L.2    Guo, Z.3
  • 48
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M., Chien, P., Naber, N., Cooke, R. and Weissman, J. S. (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428, 323-328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 49
    • 17044435107 scopus 로고    scopus 로고
    • Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins
    • Tanaka, M., Chien, P., Yonekura, K. and Weissman, J. S. (2005) Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121, 49-62
    • (2005) Cell , vol.121 , pp. 49-62
    • Tanaka, M.1    Chien, P.2    Yonekura, K.3    Weissman, J.S.4
  • 51
    • 1842786897 scopus 로고    scopus 로고
    • Core and heterogeneity of β2-microglobulin amyloid fibrils as revealed by H/D exchange
    • Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H. and Goto, Y. (2004) Core and heterogeneity of β2-microglobulin amyloid fibrils as revealed by H/D exchange. J. Mol. Biol. 338, 559-571
    • (2004) J. Mol. Biol. , vol.338 , pp. 559-571
    • Yamaguchi, K.1    Katou, H.2    Hoshino, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 52
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D. and Baldus, M. (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 102, 15871-15876
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6


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