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Volumn 45, Issue 3, 1994, Pages 373-379

Secondary structure of amyloid β peptide correlates with neurotoxic activity in vitro

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0028265912     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (401)

References (36)
  • 1
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman, R. Alzheimer's disease. N. Engl. J. Med. 314:964-972 (1986).
    • (1986) N. Engl. J. Med. , vol.314 , pp. 964-972
    • Katzman, R.1
  • 2
    • 0024556348 scopus 로고
    • Biochemistry of altered brain proteins in Alzheimer's disease
    • Selkoe, D. J. Biochemistry of altered brain proteins in Alzheimer's disease. Annu. Rev. Neurosci. 12:463-490 (1989).
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 463-490
    • Selkoe, D.J.1
  • 3
    • 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. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:885-890 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 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., E. P. Berger, and P. T. Lansbury, Jr. 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).
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 6
    • 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., A. Yasuda, P. T. M. Kenny, and M. G. Zagorski. 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).
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.G.4
  • 7
    • 0021956826 scopus 로고
    • Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome
    • Wisniewski, K., H. Wisniewski, and G. Wen. Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome. Ann. Neurol. 17:278-282 (1985).
    • (1985) Ann. Neurol. , vol.17 , pp. 278-282
    • Wisniewski, K.1    Wisniewski, H.2    Wen, G.3
  • 8
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell, J., M. Farlow, B. Ghetti, and M. Benson. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science (Washington D. C.) 254:97-99 (1991).
    • (1991) Science (Washington D. C.) , vol.254 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.4
  • 10
    • 0024990330 scopus 로고
    • Neurotropic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., L. K. Duffy, and D. A. Kirschner. Neurotropic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science (Washington D. C.) 250:279-282 (1990).
    • (1990) Science (Washington D. C.) , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 11
    • 0024543836 scopus 로고
    • Amyloid protein enhances the survival of hippocampal neurons in vitro
    • Whitson, J. S., D. J. Selkoe, and C. W. Cotman. Amyloid protein enhances the survival of hippocampal neurons in vitro. Science ( Washington D. C. ) 243:1488-1490 (1989).
    • (1989) Science ( Washington D. C. ) , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 12
    • 0026065197 scopus 로고
    • β-Amyloid from Alzheimer disease brains inhibits sprouting and survival of sympathetic neurons
    • Roher, A. E., M. J. Ball, S. V. Bhave, and A. R. Wakade. β-Amyloid from Alzheimer disease brains inhibits sprouting and survival of sympathetic neurons. Biochem. Biophys. Res. Commun. 174:572-579 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 572-579
    • Roher, A.E.1    Ball, M.J.2    Bhave, S.V.3    Wakade, A.R.4
  • 13
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M. P., B. Cheng, D. Davis, K. Bryant, I. Lieberburg, and R. Rydel. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12:376-389 (1992).
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.6
  • 15
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta-amyloid neurotoxicity
    • Busciglio, J., A. Lorenzo, and B. A. Yankner. Methodological variables in the assessment of beta-amyloid neurotoxicity. Neurobiol. Aging 13:609-612 (1992).
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 16
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., D. Burdick, A. J. Walencewicz, C. G. Glabe, and C. W. Cotman. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13:1676-1687 (1993).
    • (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
  • 17
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid are attenuated by basic FGF
    • Mattson, M. P., K. J. Tomasselli, and R. E. Rydel. Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid are attenuated by basic FGF. Brain Res. 621:35-49 (1993).
    • (1993) Brain Res. , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomasselli, K.J.2    Rydel, R.E.3
  • 18
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • Halverson, K., P. E. Frazier, D. A. Kirschner, and P. T. Lansbury, Jr. Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry 29:2693-2644 (1990).
    • (1990) Biochemistry , vol.29 , pp. 2693-12644
    • Halverson, K.1    Frazier, P.E.2    Kirschner, D.A.3    Lansbury Jr., P.T.4
  • 19
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • (V. J. Hruby, ed.), Academic Press, New York
    • Woody, R. M. Circular dichroism of peptides, in The Peptides (V. J. Hruby, ed.), Vol. 7. Academic Press, New York, 15-115 (1985).
    • (1985) The Peptides , vol.7 , pp. 15-115
    • Woody, R.M.1
  • 20
    • 0024446688 scopus 로고
    • 2+ in cerebral cortex neurons is transient in immature cells but permanent in mature cells
    • 2+ in cerebral cortex neurons is transient in immature cells but permanent in mature cells. J. Neurochem. 53: 1316-1319 (1989).
    • (1989) J. Neurochem. , vol.53 , pp. 1316-1319
    • Wahl, P.1    Schousboe, A.2    Honore, T.3    Drejer, J.4
  • 21
    • 0025799991 scopus 로고
    • An improved colorimetric assay for cell proliferation and viability utilizing the tetrazolium salt XTT
    • Roehm, N. W., G. H. Rodgers, S. M. Hatfield, and A. L. Glasebrook. An improved colorimetric assay for cell proliferation and viability utilizing the tetrazolium salt XTT. J. Immunol Methods 142:257-265 (1991).
    • (1991) J. Immunol Methods , vol.142 , pp. 257-265
    • Roehm, N.W.1    Rodgers, G.H.2    Hatfield, S.M.3    Glasebrook, A.L.4
  • 22
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J., and M. Zagorski. Solution structures of β peptide and its constituent fragments: relation to amyloid deposition. Science ( Washington D. C.) 253: 179-182 (1991).
    • (1991) Science ( Washington D. C.) , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.2
  • 23
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic β-amyloid peptide
    • Tomski, S. J., and R. M. Murphy. Kinetics of aggregation of synthetic β-amyloid peptide. Arch. Biochem. Biophys. 294:630-638 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 630-638
    • Tomski, S.J.1    Murphy, R.M.2
  • 25
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich, C., B. Kisters-Woike, J. Reed, C. L. Masters, and K. Beyreuther. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 218:149-163 (1991).
    • (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
  • 26
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • Frazier, P. E., J. T. Nguyen, W. K. Surewicz, and D. Kirschner. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 60:1190-1201 (1991).
    • (1991) Biophys. J. , vol.60 , pp. 1190-1201
    • Frazier, P.E.1    Nguyen, J.T.2    Surewicz, W.K.3    Kirschner, D.4
  • 27
    • 84901973265 scopus 로고
    • Time-dependent alterations in neurotoxicity across multiple lots of amyloid β peptide (Aβ)
    • Fuson, K. S., B. D. Gitter, G. Becker, and P. C. May. Time-dependent alterations in neurotoxicity across multiple lots of amyloid β peptide (Aβ). Neurosci. Soc. Abstr. 19:832 (1993).
    • (1993) Neurosci. Soc. Abstr. , vol.19 , pp. 832
    • Fuson, K.S.1    Gitter, B.D.2    Becker, G.3    May, P.C.4
  • 29
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., E. Rojas, and H. B. Pollard. Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci USA 90:567-571 (1993).
    • (1993) Proc. Natl. Acad. Sci USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 30
    • 84901973452 scopus 로고
    • Increased ionic conductance elicited with β amyloid peptide is dependent upon peptide secondary structure
    • Li, W. Y., and L. K. Simmons. Increased ionic conductance elicited with β amyloid peptide is dependent upon peptide secondary structure. Soc. Neurosci. Abstr. 19:1037 (1993).
    • (1993) Soc. Neurosci. Abstr. , vol.19 , pp. 1037
    • Li, W.Y.1    Simmons, L.K.2
  • 32
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the beta amyloid protein containing lesions in Alzheimer's disease and Down's syndrome
    • Snow, A. D., H. Mar, D. Nochlin, R. T. Sekiguchi, K. Kimata, Y. Koike, and T. N. Wight. Early accumulation of heparan sulfate in neurons and in the beta amyloid protein containing lesions in Alzheimer's disease and Down's syndrome. Am. J. Pathol 137:1253-1270 (1990).
    • (1990) Am. J. Pathol , vol.137 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Sekiguchi, R.T.4    Kimata, K.5    Koike, Y.6    Wight, T.N.7
  • 33
    • 0025265675 scopus 로고
    • 1-antichymotrypsin is associated solely with amyloid deposits containing the β-protein and is localized in specific cells of normal and diseased brain
    • 1-antichymotrypsin is associated solely with amyloid deposits containing the β-protein and is localized in specific cells of normal and diseased brain. Neurobiol. Aging 11:123-129 (1990).
    • (1990) Neurobiol. Aging , vol.11 , pp. 123-129
    • Abraham, C.R.1    Shirahama, T.2    Potter, H.3
  • 35
    • 0027327488 scopus 로고
    • Aluminum, iron and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide
    • Mantyh, P., J. Ghilardi, S. Rogers, E. DeMaster, C. Allen, E. Stimson, and J. Maggio. Aluminum, iron and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J. Neurochem. 61:1171-1174 (1993).
    • (1993) J. Neurochem. , vol.61 , pp. 1171-1174
    • Mantyh, P.1    Ghilardi, J.2    Rogers, S.3    Demaster, E.4    Allen, C.5    Stimson, E.6    Maggio, J.7
  • 36
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
    • Ghiso, J., E. Matsubara, A. Koudinov, N. Choi-Miura, M. Tomita, T. Wisniewski, and B. Frangione. The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem. J. 293:27-30 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Choi-Miura, N.4    Tomita, M.5    Wisniewski, T.6    Frangione, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.