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Volumn 256, Issue 3, 1998, Pages 560-569

The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's β-amyloid peptide

Author keywords

A aggregation; Alzheimer's disease; Amyloid; Secondary structure

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0032530466     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560560.x     Document Type: Article
Times cited : (41)

References (50)
  • 1
    • 0025879957 scopus 로고
    • An in vivo model for the neurodegenerative effects of β amyloid and protection by substance P
    • Kowall, N. W., Beal, M. F., Busciglio, J., Duffy, L. K. & Yankner, B. A. (1991) An in vivo model for the neurodegenerative effects of β amyloid and protection by substance P, Proc. Natl Acad. Sci. USA 88, 7247-7251.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7247-7251
    • Kowall, N.W.1    Beal, M.F.2    Busciglio, J.3    Duffy, L.K.4    Yankner, B.A.5
  • 2
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K. & Kirschner, D. A. (1990) Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides, Science 250, 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 3
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G. & Cotman, C. W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state, J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 6
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C. J., Walencewicz, A. J., Glabe, C. G. & Cotman, C. W. (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
  • 8
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J. & Zagorski, M. G. (1991) Solution structures of β peptide and its constituent fragments: relation to amyloid deposition, Science 253, 179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 9
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow, C. J., Yasuda, A., Kenny, P. T. M. & Zagorski, M. Q. (1992) Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. Analysis of circular dichroism spectra, J. Mol. Biol. 225, 1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.Q.4
  • 11
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of β-amyloid peptide in vitro
    • Pike, C. J., Overman, M. J. & Cotman, C. W. (1995) Amino-terminal deletions enhance aggregation of β-amyloid peptide in vitro, J. Biol. Chem. 270, 23895-23898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 12
    • 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
  • 13
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T. Jr (1993) The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease, Biochemistry 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 14
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-region to aggregation and neurotoxicity
    • Pike, C. J., Walencewicz-Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G. & Cotman, C. W. (1995) Structure-activity analyses of β-amyloid peptides: contributions of the β25-region to aggregation and neurotoxicity, J. Neurochem. 64, 253-265.
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 16
    • 0027427734 scopus 로고
    • Toxic effect of a β-amyloid peptide β (22-35) on the hippocampal neuron and its prevention
    • Takadera, T., Sakura, N., Mohri, T. & Hashimoto, T. (1993) Toxic effect of a β-amyloid peptide β (22-35) on the hippocampal neuron and its prevention, Neurosci. Lett. 161, 41-44.
    • (1993) Neurosci. Lett. , vol.161 , pp. 41-44
    • Takadera, T.1    Sakura, N.2    Mohri, T.3    Hashimoto, T.4
  • 17
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at Ser residue
    • Kaneko, I., Yamada, N., Sakuraba, Y., Kamenosono, M. & Tutumi, S. (1995) Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at Ser residue, J. Neurochem. 65, 2585-2593.
    • (1995) J. Neurochem. , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Sakuraba, Y.3    Kamenosono, M.4    Tutumi, S.5
  • 18
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein e and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation
    • Golabek, A. A., Soto, C., Vogel, T. & Wisniewski, T. (1996) The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation, J. Biol. Chem. 271, 10602-10606.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 22
    • 0026045862 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine tor glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski, T. Ghiso, J. & Frangione, B. (1991) Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine tor glutamic acid substitution have accelerated amyloid fibril formation, Biochem. Biophys. Res. Commun. 179, 1247-1254.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 23
    • 0027330265 scopus 로고
    • Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide
    • Clements, A., Walsh, D. M., Williams, C. H. & Allsop, D. (1993) Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide, Neurosci. Lett. 161, 17-20.
    • (1993) Neurosci. Lett. , vol.161 , pp. 17-20
    • Clements, A.1    Walsh, D.M.2    Williams, C.H.3    Allsop, D.4
  • 24
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and metal-binding properties of mutant forms of the amyloid Aβ peptide of Alzheimer's disease
    • Clements, A., Allsop, D., Walsh, D. M. & Williams, C. H. (1996) Aggregation and metal-binding properties of mutant forms of the amyloid Aβ peptide of Alzheimer's disease, J. Neurochem. 66, 740-747.
    • (1996) J. Neurochem. , vol.66 , pp. 740-747
    • Clements, A.1    Allsop, D.2    Walsh, D.M.3    Williams, C.H.4
  • 25
    • 0029916711 scopus 로고    scopus 로고
    • The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis
    • Soto, C. & Castano, E. M. (1996) The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis, Biochem. J. 314, 701-707.
    • (1996) Biochem. J. , vol.314 , pp. 701-707
    • Soto, C.1    Castano, E.M.2
  • 26
    • 0028246308 scopus 로고
    • Mutations associated with a locus for Familial Alzheimer's Disease result in alternative processing of amyloid β-protein precursor
    • Haass, C., Hung, A. Y., Selkoe, D. J. & Teplow, D. B. (1994) Mutations associated with a locus for Familial Alzheimer's Disease result in alternative processing of amyloid β-protein precursor, J. Biol. Chem. 269, 17741-17748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 28
    • 0029945024 scopus 로고    scopus 로고
    • Cellular MTT reduction distinguishes the mechanism of action of β-amyloid from that of tachykinin receptor peptides
    • Sherman, M. S. (1996) Cellular MTT reduction distinguishes the mechanism of action of β-amyloid from that of tachykinin receptor peptides, Neuropeptides 30, 125-132.
    • (1996) Neuropeptides , vol.30 , pp. 125-132
    • Sherman, M.S.1
  • 29
    • 0003363148 scopus 로고
    • The synthesis of some peptides related to the amyloid β peptide 25-35: Use of N-(2-hydroxy-4-methoxybenzyl) protection
    • El-Agnaf, O. M. A., Harriott, P., Guthrie, D. J. S., Irvine, G. B. & Walker, B. (1994) The synthesis of some peptides related to the amyloid β peptide 25-35: use of N-(2-hydroxy-4-methoxybenzyl) protection, Lett. Pept. Sci. 1, 135-141.
    • (1994) Lett. Pept. Sci. , vol.1 , pp. 135-141
    • El-Agnaf, O.M.A.1    Harriott, P.2    Guthrie, D.J.S.3    Irvine, G.B.4    Walker, B.5
  • 30
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • Selkoe, D. J. (1994) Normal and abnormal biology of the β-amyloid precursor protein, Annu. Rev. Neurosci. 17, 489-517.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 31
    • 0028181758 scopus 로고
    • Reversible random coil-β-sheet transition of the Alzheimer's β-amyloid fragment (25-35)
    • Terzi, E., Holzemann, G. & Seelig, J. (1994) Reversible random coil-β-sheet transition of the Alzheimer's β-amyloid fragment (25-35), Biochemistry 33, 1345-1350.
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 32
    • 0028179865 scopus 로고
    • Alzhemier β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi, K., Holzemann, G. & Seelig, J. (1994) Alzhemier β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes, Biochemistry 33, 7434-7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, K.1    Holzemann, G.2    Seelig, J.3
  • 34
    • 0029556962 scopus 로고
    • Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid β (25-35) peptide as analyzed by single alanine substitution
    • Sato, K., Wakamiya, A., Maeda, T., Noguchi, K., Takashima, A. & Imahori, K. (1995) Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid β (25-35) peptide as analyzed by single alanine substitution, J. Biochem. 118, 1108-1111.
    • (1995) J. Biochem. , vol.118 , pp. 1108-1111
    • Sato, K.1    Wakamiya, A.2    Maeda, T.3    Noguchi, K.4    Takashima, A.5    Imahori, K.6
  • 36
    • 0028980362 scopus 로고
    • The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation
    • Soto, C., Castano, E. M., Frangione, B. & Inestrosa, N. C. (1995) The α-helical to β-strand transition in the amino-terminal fragment of the amyloid β-peptide modulates amyloid formation, J. Biol. Chem. 270, 3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 38
    • 0028180518 scopus 로고
    • A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer's disease
    • Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. K. Floyd, R. A. & Butterfield, D. A. (1994) A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer's disease, Proc. Natl Acad. Sci. USA 91, 3270-3274.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.4    Harris, M.5    Wu, J.K.6    Floyd, R.A.7    Butterfield, D.A.8
  • 42
    • 0028971326 scopus 로고
    • Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure
    • Soto, C., Castano, E. M., Kumar, R. A., Beavis, R. C. & Frangione, B. (1995) Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure, Neurosci. Lett. 200, 105-108.
    • (1995) Neurosci. Lett. , vol.200 , pp. 105-108
    • Soto, C.1    Castano, E.M.2    Kumar, R.A.3    Beavis, R.C.4    Frangione, B.5
  • 43
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acid residues reduce the amyloidogenicity of Alzheimer's disease βA4 peptides
    • Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C. L. & Beyreuther, K. (1992) Substitutions of hydrophobic amino acid residues reduce the amyloidogenicity of Alzheimer's disease βA4 peptides, J. Mol. Biol. 228, 460-473.
    • (1992) J. Mol. Biol. , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 44
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M. & Teplow, D. B. (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
  • 45
    • 0028179341 scopus 로고
    • Chemical characterisation of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • Gowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P. & Ball, M. J. (1994) Chemical characterisation of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease, J. Biol. Chem. 269, 10987-10990.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10987-10990
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3    Cotter, R.J.4    Chaney, M.5    Little, S.P.6    Ball, M.J.7
  • 46
    • 0030035922 scopus 로고    scopus 로고
    • P3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain
    • Higgins, L. S., Murphy, G. M., Forno, L. S., Catalano, R. & Cordell, B. (1996) p3 β-amyloid peptide has a unique and potentially pathogenic immunohistochemical profile in Alzheimer's disease brain, Am. J. Pathol. 149, 585-596.
    • (1996) Am. J. Pathol. , vol.149 , pp. 585-596
    • Higgins, L.S.1    Murphy, G.M.2    Forno, L.S.3    Catalano, R.4    Cordell, B.5
  • 48
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood, S. J., Maleeff, B., Hart, T. & Wetzel, R. (1996) Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ, J. Mol. Biol. 256, 870-877.
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 49
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett, J. T. & Lansbury, P. T. Jr (1992) Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB, Biochemistry 31, 12345-12352.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 50
    • 0029854533 scopus 로고    scopus 로고
    • Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence
    • Esler, W. P., Stimson, E. R., Ghilardi, Lu, Y.-A., Felix, A. M., Vinters, H. V., J. R., Mantyh, P. W., Lee, J. P. & Maggio, J. E. (1996) Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence, Biochemistry 35, 13914-13921.
    • (1996) Biochemistry , vol.35 , pp. 13914-13921
    • Esler, W.P.1    Stimson, E.R.2    Ghilardi3    Lu, Y.-A.4    Felix, A.M.5    Vinters, H.V.J.R.6    Mantyh, P.W.7    Lee, J.P.8    Maggio, J.E.9


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