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Volumn 76, Issue 6, 1999, Pages 2871-2878

An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0033040551     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77442-4     Document Type: Article
Times cited : (113)

References (52)
  • 2
    • 0031018393 scopus 로고    scopus 로고
    • De novo design of native proteins: Characterization of proteins intended to fold into anti-parallel, rod-like, four-helix bundles
    • Betz, S. F., P. A. Liebman, and W. F. DeGrado. 1997. De novo design of native proteins: characterization of proteins intended to fold into anti-parallel, rod-like, four-helix bundles. Biochemistry. 36:2450-2458.
    • (1997) Biochemistry. , vol.36 , pp. 2450-2458
    • Betz, S.F.1    Liebman, P.A.2    DeGrado, W.F.3
  • 3
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8
    • Blake, C. C., M. J. Geisow, S. J. Oatley, B. Rerat, and C. Rerat. 1978. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J. Mol. Biol. 121:339-356.
    • (1978) Å. J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 4
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron x-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C., and L. Serpell. 1996. Synchrotron x-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure. 4:989-998.
    • (1996) Structure. , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 5
    • 0028588694 scopus 로고
    • Congo red protects against toxicity of β-amyloid peptides on rat hippocampal neurones
    • Burgevin, M. C., M. Passat, N. Daniel, M. Capet, and A. Doble. 1994. Congo red protects against toxicity of β-amyloid peptides on rat hippocampal neurones. Neuroreport. 5:2429-2432.
    • (1994) Neuroreport. , vol.5 , pp. 2429-2432
    • Burgevin, M.C.1    Passat, M.2    Daniel, N.3    Capet, M.4    Doble, A.5
  • 6
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils
    • Carter, D. B., and K. C. Chou. 1998. A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils. Neurobiol. Aging. 19:37-44.
    • (1998) Neurobiol. Aging. , vol.19 , pp. 37-44
    • Carter, D.B.1    Chou, K.C.2
  • 7
    • 0027280172 scopus 로고
    • Congo red inhibition of scrapie agent replication
    • Caughey, B., D. Ernst, and R. E. Race. 1993. Congo red inhibition of scrapie agent replication. J. Virol. 67:6270-6272.
    • (1993) J. Virol. , vol.67 , pp. 6270-6272
    • Caughey, B.1    Ernst, D.2    Race, R.E.3
  • 8
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease
    • Chancy, M. O., S. D. Webster, Y. M. Kuo, and A. E. Roher. 1998. Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Eng. 11:761-767.
    • (1998) Protein Eng. , vol.11 , pp. 761-767
    • Chancy, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 10
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide (1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • Coles, M., W. Bicknell, A. A. Watson, D. P. Fairlie, and D. J. Craik. 1998. Solution structure of amyloid β-peptide (1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry. 37:11064-11077.
    • (1998) Biochemistry. , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 11
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods
    • Cooper, J. H. 1974. Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Lab. Invest. 31: 232-238.
    • (1974) Lab. Invest. , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 13
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N·log(N) method for Ewald sums. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 14
    • 0014346532 scopus 로고
    • Histochemical observations on amyloid with reference to polarization microscopy
    • DeLellis, R. A., G. G. Glenner, and J. S. Ram. 1968. Histochemical observations on amyloid with reference to polarization microscopy. J. Histochem. Cytochem. 16:663-665.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 663-665
    • Delellis, R.A.1    Glenner, G.G.2    Ram, J.S.3
  • 15
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. 1990. Dominant forces in protein folding. Biochemistry. 29: 7133-7155.
    • (1990) Biochemistry. , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 16
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • Fraser, P. E., J. T. Nguyen, W. K. Surewicz, and D. A. Kirschner. 1991. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 60:1190-1201.
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Fraser, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.A.4
  • 17
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G., and C. W. Wong. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 19
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J. D., C. M. Lieber, and P. T. Lansbury, Jr. 1997. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4:951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury P.T., Jr.3
  • 20
    • 0026101636 scopus 로고
    • Aggregration and secondary structure of synthetic amyloid β-A4 peptides of Alzheimer's disease
    • Hilbich, C., B. Kisters-Woike, J. Reed, C. L. Masters, and K. Beyreuther. 1991. Aggregration and secondary structure of synthetic amyloid β-A4 peptides of Alzheimer's disease. J. Mol. Biol. 218:149-163.
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 21
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by x-ray diffraction
    • Inouye, H., P. E. Fraser, and D. A. Kirschner. 1993. Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: analysis by x-ray diffraction. Biophys. J. 64:502-519.
    • (1993) Biophys. J. , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 22
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogensis of Alzheimer's disease
    • Jarrett, J. T., E. P. Berger, and P. T. Lansbury, Jr. 1993. The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogensis of Alzheimer's disease. Biochemistry. 32:4693-4698.
    • (1993) Biochemistry. , vol.32 , pp. 4693-4698
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 24
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 25
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to β-protein from Alzheimer disease forms amyloid-like fibrils in vitro
    • Kirschner, D. A., H. Inouye, L. K. Duffy, A. Sinclair, M. Lind, and D. J. Selkoe. 1987. Synthetic peptide homologous to β-protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA. 84:6953-8957.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6953-8957
    • Kirschner, D.A.1    Inouye, H.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 26
    • 0024363054 scopus 로고
    • Two simple methods for quantifying low-affinity dye-substrate binding
    • Klunk, W. E., J. W. Pettegrew, and D. J. Abraham. 1989. Two simple methods for quantifying low-affinity dye-substrate binding. J. Histochem. Cytochem. 37:1293-1297.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1293-1297
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 28
    • 0032080907 scopus 로고    scopus 로고
    • Interaction of transmembrane helices by a knobs-into-holes packing characteristic of soluble coiled coils
    • Langosch, D., and J. Heringa. 1998. Interaction of transmembrane helices by a knobs-into-holes packing characteristic of soluble coiled coils. Proteins. 3:150-159.
    • (1998) Proteins. , vol.3 , pp. 150-159
    • Langosch, D.1    Heringa, J.2
  • 29
    • 0026693596 scopus 로고
    • In pursuit of the molecular structure of amyloid plaque: New technology provides unexpected and critical information
    • Lansbury, P. T., Jr. 1992. In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information. Biochemistry. 31:6865-6870.
    • (1992) Biochemistry. , vol.31 , pp. 6865-6870
    • Lansbury P.T., Jr.1
  • 31
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo, N. D., and D. T. Downing. 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry. 37:1731-1735.
    • (1998) Biochemistry. , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 34
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin, A., D. S. Chung, G. B. Benedek, D. A. Kirschner, and D. B. Teplow. 1996. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA. 93:1125-1129.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 35
    • 0028172886 scopus 로고
    • β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo, A., and B. A. Yankner. 1994. β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA. 91:12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 36
    • 0031766850 scopus 로고    scopus 로고
    • Molecular simulation of the primary and secondary structures of the Aβ (1-42) peptide of Alzheimer's disease
    • Mager, P. P. 1998. Molecular simulation of the primary and secondary structures of the Aβ (1-42) peptide of Alzheimer's disease. Med. Res. Rev. 18:403-430.
    • (1998) Med. Res. Rev. , vol.18 , pp. 403-430
    • Mager, P.P.1
  • 37
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β (1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B., H. Inouye, K. E. Szumowski, and D. A. Kirschner. 1998. Structural analysis of Alzheimer's β (1-40) amyloid: protofilament assembly of tubular fibrils. Biophys. J. 74:537-545.
    • (1998) Biophys. J. , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 38
    • 0000573263 scopus 로고
    • Configuration of polypeptide chains with favored orientation around single bonds: Two new pleated sheets
    • Pauling, L., and R. Corey. 1951. Configuration of polypeptide chains with favored orientation around single bonds: two new pleated sheets. Proc. Natl. Acad. Sci. USA. 37:729-739.
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 729-739
    • Pauling, L.1    Corey, R.2
  • 39
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro
    • Pike, C., M. J. Overman, and C. W. Cotman. 1995. Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. J. Biol. Chem. 270:23895-23898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.1    Overman, M.J.2    Cotman, C.W.3
  • 40
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C. J., A. J. Walencewicz, C. G. Glabe, and C. W. Cotman. 1991. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563:311-314.
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 41
    • 0029117593 scopus 로고
    • Sulfonated dyes attenuate the toxic effects of β-amyloid in a structure-specific fashion
    • Pollack, S. J., I. I. Sadler, S. R. Hawtin, V. J. Tailor, and M. S. Shearman. 1995. Sulfonated dyes attenuate the toxic effects of β-amyloid in a structure-specific fashion. Neurosci. Lett. 197:211-214.
    • (1995) Neurosci. Lett. , vol.197 , pp. 211-214
    • Pollack, S.J.1    Sadler, I.I.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 42
    • 0000880131 scopus 로고
    • On the binding of Congo red by amyloid
    • Puchtler, H., F. Sweat, and M. Levine. 1962. On the binding of Congo red by amyloid. J. Histochem. 10:355-364.
    • (1962) J. Histochem. , vol.10 , pp. 355-364
    • Puchtler, H.1    Sweat, F.2    Levine, M.3
  • 43
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe, D. J. 1996. Amyloid β-protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271:18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 44
  • 46
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar a β-amyloid in rat brain
    • Snow, A. D., R. Sekiguchi, D. Nochlin, P. Fraser, K. Kimata, A. Mizutani, M. Arai, W. A. Schreier, and D. G. Morgan. 1994. An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A β-amyloid in rat brain. Neuron. 12:219-234.
    • (1994) Neuron. , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 50
    • 0026451628 scopus 로고
    • Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences
    • Turnell, W. G., and J. T. Finch. 1992. Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J. Mol. Biol. 20:1205-1223.
    • (1992) J. Mol. Biol. , vol.20 , pp. 1205-1223
    • Turnell, W.G.1    Finch, J.T.2
  • 51
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh, D. M., A. Lomakin, G. B. Benedek, M. M. Condron, and D. B. Teplow. 1997. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272:22364-22372.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 52
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood, S. J., R. Wetzel, J. D. Martin, and M. R. Hurle. 1995. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry. 34:724-730.
    • (1995) Biochemistry. , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4


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