메뉴 건너뛰기




Volumn 69, Issue 3, 1997, Pages 1204-1212

Selective aggregation of endogenous β-amyloid peptide and soluble amyloid precursor protein in cerebrospinal fluid by zinc

Author keywords

Aggregation; Alzheimer's disease; Amyloid deposit; Brain; Cerebrospinal fluid; Zinc; Amyloid peptide

Indexed keywords

AMYLOID BETA PROTEIN; ZINC;

EID: 0030757388     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69031204.x     Document Type: Article
Times cited : (59)

References (76)
  • 1
    • 0025265675 scopus 로고
    • Alpha 1-antichymotrypsin is associated solely with amyloid deposits containing the beta-protein. Amyloid and cell localization of alpha 1-antichymotrypsin
    • Abraham C. R., Shirahama T., and Potter H. (1990) Alpha 1-antichymotrypsin is associated solely with amyloid deposits containing the beta-protein. Amyloid and cell localization of alpha 1-antichymotrypsin. Neurobiol. Aging 11, 123-129.
    • (1990) Neurobiol. Aging , vol.11 , pp. 123-129
    • Abraham, C.R.1    Shirahama, T.2    Potter, H.3
  • 2
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • 2+ from brain tissue during activity. Nature 308, 734-736.
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 3
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease: Analysis of circular dichroism spectra
    • Barrow C. J., Yasuda A., Kenny P. T., and Zagorski M. G. (1992) Solution conformations and aggregational properties of synthetic amyloid beta-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.3    Zagorski, M.G.4
  • 5
    • 0029975425 scopus 로고    scopus 로고
    • Evaluation of cathepsins D and G and EC 3.4.24.15 as candidate β-secretase proteases using peptide and amyloid precursor protein substrates
    • Brown A. M., Tummolo D. M., Spruyt M. A., Jacobsen J. S., and Sonnenberg-Reines J. L. (1996) Evaluation of cathepsins D and G and EC 3.4.24.15 as candidate β-secretase proteases using peptide and amyloid precursor protein substrates. J. Neurochem. 66, 2436-2445.
    • (1996) J. Neurochem. , vol.66 , pp. 2436-2445
    • Brown, A.M.1    Tummolo, D.M.2    Spruyt, M.A.3    Jacobsen, J.S.4    Sonnenberg-Reines, J.L.5
  • 10
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and metal-binding properties of mutant forms of amyloid Aβ peptide of Alzheimer's disease
    • Clements A., Allsop D., Walsh D. M., and Williams C. H. (1996) Aggregation and metal-binding properties of mutant forms of 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
  • 11
    • 0027332522 scopus 로고
    • β-Amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease
    • Cummings B. J., Su J. H., Cotman C. W., White R., and Russel M. J. (1993) β-Amyloid accumulation in aged canine brain: a model of early plaque formation in Alzheimer's disease. Neurobiol. Aging 14, 547-560.
    • (1993) Neurobiol. Aging , vol.14 , pp. 547-560
    • Cummings, B.J.1    Su, J.H.2    Cotman, C.W.3    White, R.4    Russel, M.J.5
  • 13
    • 0022388387 scopus 로고
    • The dithizone, Timm's sulphide silver and the selenium methods demonstrate a chelatable pool of zinc in CNS. A proton activation (PIXE) analysis of carbon tetrachloride extracts from rat brains and spinal cords intravitally treated with dithizone
    • Danscher G., Howell G. A., Perez-Clausell J., and Hertel N. (1985) The dithizone, Timm's sulphide silver and the selenium methods demonstrate a chelatable pool of zinc in CNS. A proton activation (PIXE) analysis of carbon tetrachloride extracts from rat brains and spinal cords intravitally treated with dithizone. Histochemistry 83, 419-422.
    • (1985) Histochemistry , vol.83 , pp. 419-422
    • Danscher, G.1    Howell, G.A.2    Perez-Clausell, J.3    Hertel, N.4
  • 17
    • 0025838381 scopus 로고
    • pH-dependent structural transitions of Alzheimer amyloid peptides
    • Fraser P. E., Nguyen J. T., Surewicz W. K., and Kirschner D. A. (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
  • 18
    • 0026070054 scopus 로고
    • Effects of injected Alzheimer beta-amyloid cores in rat brain
    • Frautschy S. A., Baird A., and Cole G. M. (1991) Effects of injected Alzheimer beta-amyloid cores in rat brain. Proc. Natl. Acad. Sci. USA 88, 8362-8366.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8362-8366
    • Frautschy, S.A.1    Baird, A.2    Cole, G.M.3
  • 19
    • 0024779411 scopus 로고
    • Neurobiology of zinc-containing neurons
    • Frederickson C. J. (1989) Neurobiology of zinc-containing neurons. Int. Rev. Neurobiol. 31, 145-238.
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 20
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
    • Ghiso J., Matsubara E., Koudinov A., Choi-Miura N. H., Tomita M., Wisniewski T., and Frangione B. (1993) The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem. J. 293, 27-30.
    • (1993) Biochem. J. , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Choi-Miura, N.H.4    Tomita, M.5    Wisniewski, T.6    Frangione, B.7
  • 21
    • 0021256895 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril 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
  • 22
    • 0015408029 scopus 로고
    • Infrared spectroscopy of human amyloid fibrils and immunoglobulin proteins
    • Glenner G. G., Eanes E. D., and Page D. L. (1972) Infrared spectroscopy of human amyloid fibrils and immunoglobulin proteins. J. Histochem. Cytochem. 20, 821-826.
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 24
    • 0020517761 scopus 로고
    • Cerebrospinal fluid trace element content in dementia: Clinical, radiologic, and pathologic correlations
    • Hershey C. O., Hershey L. A., Varnes A., Vibhakar S. D., Lavin P., and Strain H. (1983) Cerebrospinal fluid trace element content in dementia: clinical, radiologic, and pathologic correlations. Neurology 33, 1350-1353.
    • (1983) Neurology , vol.33 , pp. 1350-1353
    • Hershey, C.O.1    Hershey, L.A.2    Varnes, A.3    Vibhakar, S.D.4    Lavin, P.5    Strain, H.6
  • 25
    • 0026101636 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich C., Kisters-Woike B., Reed J., Masters C. L., and Beyreuther K. (1991) Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. 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
  • 26
    • 0021220724 scopus 로고
    • Stimulation-induced uptake and release of zinc in hippocampal slices
    • Howell G. A., Welch M., and Frederickson C. J. (1984) Stimulation-induced uptake and release of zinc in hippocampal slices. Nature 308, 736-738.
    • (1984) Nature , vol.308 , pp. 736-738
    • Howell, G.A.1    Welch, M.2    Frederickson, C.J.3
  • 27
    • 0025853543 scopus 로고
    • Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis
    • Johnstone E. M., Chancy M. O., Norris F. H., Pascual R., and Little S. P. (1991) Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis. Mol. Brain Res. 10, 299-305.
    • (1991) Mol. Brain Res. , vol.10 , pp. 299-305
    • Johnstone, E.M.1    Chancy, M.O.2    Norris, F.H.3    Pascual, R.4    Little, S.P.5
  • 28
    • 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., and 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
  • 30
    • 0029777299 scopus 로고    scopus 로고
    • The role of zinc in selective neuronal death after transient global cerebral ischemia
    • Koh J. Y., Suh S. W., Gwag B. J., He Y. Y., Hsu C. Y., and Choi D. W. (1996) The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 272, 1013-1016.
    • (1996) Science , vol.272 , pp. 1013-1016
    • Koh, J.Y.1    Suh, S.W.2    Gwag, B.J.3    He, Y.Y.4    Hsu, C.Y.5    Choi, D.W.6
  • 31
    • 0025879957 scopus 로고
    • An in vivo model for the neurodegenerative effects of beta amyloid and protection by substance P
    • Kowall N. W., Beal M. F., Busciglio J., Duffy L. K., and Yankner B. A. (1991) An in vivo model for the neurodegenerative effects of beta 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
  • 35
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A. and Yankner B. (1994) Beta-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.2
  • 36
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein e promote assembly of Alzheimer beta-protein into filaments
    • Ma J., Yee A., Brewer H. B., Das S., and Potter H. (1994) Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments [see comments]. Nature 372, 92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 38
    • 0027327488 scopus 로고
    • Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide
    • Mantyh P. W., Ghilardi J. R., Rogers S., DeMaster E., Allen C. J., Stimson E. R., and Maggio J. (1993) Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J. Neurochem. 61, 1171-1174.
    • (1993) J. Neurochem. , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3    Demaster, E.4    Allen, C.J.5    Stimson, E.R.6    Maggio, J.7
  • 40
    • 0027520019 scopus 로고
    • Intrinsic stoichiometric equilibrium constants for the binding of zinc (II) and copper (II) to the high affinity site of serum albumin
    • Masuoka J., Henegenauer J., Van Dyke B. R., and Saltman P. (1993) Intrinsic stoichiometric equilibrium constants for the binding of zinc (II) and copper (II) to the high affinity site of serum albumin. J. Biol. Chem. 268, 21533-21537.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21533-21537
    • Masuoka, J.1    Henegenauer, J.2    Van Dyke, B.R.3    Saltman, P.4
  • 41
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's A beta interaction
    • Matsubara E., Frangione B., and Ghiso J. (1995) Characterization of apolipoprotein J-Alzheimer's A beta interaction. J. Biol. Chem. 270, 7563-7567.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3
  • 42
    • 0028806980 scopus 로고
    • Apolipoproteins E3 and E4 induce, and transthyretin prevents accumulation of the Alzheimer's beta-amyloid peptide in cultured vascular smooth muscle cells
    • Mazur-Kolecka B., Frackowiak J., and Wisniewski T. (1995) Apolipoproteins E3 and E4 induce, and transthyretin prevents accumulation of the Alzheimer's beta-amyloid peptide in cultured vascular smooth muscle cells. Brain Res. 698, 217-222.
    • (1995) Brain Res. , vol.698 , pp. 217-222
    • Mazur-Kolecka, B.1    Frackowiak, J.2    Wisniewski, T.3
  • 44
    • 0024370108 scopus 로고
    • Relationships among the cerebral amyloid peptides and their precursors
    • Miller D. L., Currie J. R., Iqbal K., Potempska A., and Styles J. (1989) Relationships among the cerebral amyloid peptides and their precursors. Ann. Med. 21, 83-87.
    • (1989) Ann. Med. , vol.21 , pp. 83-87
    • Miller, D.L.1    Currie, J.R.2    Iqbal, K.3    Potempska, A.4    Styles, J.5
  • 45
    • 0027984643 scopus 로고
    • Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP)
    • Multhaup G., Bush A. I., Pollwein P., and Masters C. L. (1994) Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP). FEBS Lett. 355, 151-154.
    • (1994) FEBS Lett. , vol.355 , pp. 151-154
    • Multhaup, G.1    Bush, A.I.2    Pollwein, P.3    Masters, C.L.4
  • 48
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation
    • Pike C. J., Walencewicz A. J., Glabe C. G., and Cotman C. W. (1991) In vitro aging of beta-amyloid protein causes peptide aggregation. 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
  • 49
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C. J., Burdick D., Walencewicz A. J., Glabe C. G., and Cotman C. W. (1993) Neurodegeneration induced by beta-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
  • 50
    • 0028170719 scopus 로고
    • Cerebrospinal fluid concentrations of soluble amyloid beta-protein and apolipoprotein e in patients with Alzheimer's disease: Correlations with amyloid load in the brain
    • Pirttilla T., Kim K. S., Mehta P., Frey H., and Wisniewski H. M. (1994) Cerebrospinal fluid concentrations of soluble amyloid beta-protein and apolipoprotein E in patients with Alzheimer's disease: correlations with amyloid load in the brain. J. Neurol. Sci. 127, 90-95.
    • (1994) J. Neurol. Sci. , vol.127 , pp. 90-95
    • Pirttilla, T.1    Kim, K.S.2    Mehta, P.3    Frey, H.4    Wisniewski, H.M.5
  • 51
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli F., Castano E., Glenner G. G., and Frangione B. (1988) Differences between vascular and plaque core amyloid in Alzheimer's disease. J. Neurochem. 51, 648-651.
    • (1988) J. Neurochem. , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3    Frangione, B.4
  • 52
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher A. E., Wolfe D., Palutke M., and Kukuruga D. (1986) Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Proc. Natl. Acad. Sci. USA 83, 2662-2666.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2662-2666
    • Roher, A.E.1    Wolfe, D.2    Palutke, M.3    Kukuruga, D.4
  • 53
    • 0026065197 scopus 로고
    • Beta-amyloid from Alzheimer disease brains inhibits sprouting and survival of sympathetic neurons
    • Roher A. E., Ball M. J., Bhave S.V., and Wakade A. R. (1991) Beta-amyloid from Alzheimer disease brains inhibits sprouting and survival of sympathetic neurons. Biochem. Biophys. Res. Commun. 174, 572-579.
    • (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
  • 54
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H. and von Jagow G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 56
    • 0027220007 scopus 로고
    • Extracellular and cerebrospinal fluids
    • Segal M. B. (1993) Extracellular and cerebrospinal fluids. J. Inherit. Metab. Dis. 16, 617-638.
    • (1993) J. Inherit. Metab. Dis. , vol.16 , pp. 617-638
    • Segal, M.B.1
  • 57
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D. J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 61
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome
    • Snow A. D., Mar H., Noclin D., Sekiguchi R. T., Kimata K., Koike Y., and Wight T. N. (1990) Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome. Am. J. Pathol. 137, 1253-1270.
    • (1990) Am. J. Pathol. , vol.137 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Noclin, D.3    Sekiguchi, R.T.4    Kimata, K.5    Koike, Y.6    Wight, T.N.7
  • 62
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain
    • Snow A. D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mizutani A., Arai M., Schreier W. A., and Morgan D. G. (1994) An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-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
  • 63
    • 0026646280 scopus 로고
    • Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat
    • Stephenson D. T., Rash K., and Clemens J. (1992) Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat. Brain Res. 593, 128-135.
    • (1992) Brain Res. , vol.593 , pp. 128-135
    • Stephenson, D.T.1    Rash, K.2    Clemens, J.3
  • 64
    • 12044254746 scopus 로고
    • Binding of human apolipoprotein e to synthetic amyloid beta peptide: Isoform-specific effects and implications for late-onset Alzheimer's disease
    • Strittmatter W. J., Saunders A. M., Schenechel D., Pericak-Vance M., Enghild J., Slavesen G. S., and Roses A. D. (1993a) Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer's disease. Proc. Natl. Acad. Sci. USA 90, 8098-8102.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8098-8102
    • Strittmatter, W.J.1    Saunders, A.M.2    Schenechel, D.3    Pericak-Vance, M.4    Enghild, J.5    Slavesen, G.S.6    Roses, A.D.7
  • 67
    • 0026761857 scopus 로고
    • Senile plaques in cerebral amyloid angiopathy show accumulation of amyloid precursor protein without cytoskeletal abnormalities
    • Tabaton M., Cammarata S., Mandybur T., Richey P., Kawai M., Perry G., and Gambetti P. (1992) Senile plaques in cerebral amyloid angiopathy show accumulation of amyloid precursor protein without cytoskeletal abnormalities. Brain Res. 593, 299-303.
    • (1992) Brain Res. , vol.593 , pp. 299-303
    • Tabaton, M.1    Cammarata, S.2    Mandybur, T.3    Richey, P.4    Kawai, M.5    Perry, G.6    Gambetti, P.7
  • 68
    • 0025138527 scopus 로고
    • Possible role of zinc in the selective degeneration of hilar neurons after cerebral ischemia in the adult rat
    • Tonder N., Johansen F. F., Frederickson C. J., Zimmer J., and Diemer N. H. (1990) Possible role of zinc in the selective degeneration of hilar neurons after cerebral ischemia in the adult rat. Neurosci. Lett. 109, 247-252.
    • (1990) Neurosci. Lett. , vol.109 , pp. 247-252
    • Tonder, N.1    Johansen, F.F.2    Frederickson, C.J.3    Zimmer, J.4    Diemer, N.H.5
  • 69
    • 0028807286 scopus 로고
    • Serum zinc, senile plaques, and neurofibrillary tangles: Findings from the Nun study
    • Tully C. L., Snowdon D. A., and Markesbery W. R. (1995) Serum zinc, senile plaques, and neurofibrillary tangles: findings from the Nun study. Neuroreport 6, 2105-2108.
    • (1995) Neuroreport , vol.6 , pp. 2105-2108
    • Tully, C.L.1    Snowdon, D.A.2    Markesbery, W.R.3
  • 71
    • 0026493941 scopus 로고
    • Regional accumulation of amyloid beta/A4 protein precursor in the gerbil brain following transient cerebral ischemia
    • Wakita H., Tomimoto H., Akiguchi I., Ohnishi K., Nakamura S., and Kimura J. (1992) Regional accumulation of amyloid beta/A4 protein precursor in the gerbil brain following transient cerebral ischemia. Neurosci. Lett. 146, 135-138.
    • (1992) Neurosci. Lett. , vol.146 , pp. 135-138
    • Wakita, H.1    Tomimoto, H.2    Akiguchi, I.3    Ohnishi, K.4    Nakamura, S.5    Kimura, J.6
  • 72
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T. and Frangione B. (1992) Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci. Lett. 135, 235-238.
    • (1992) Neurosci. Lett. , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 73
    • 0029836629 scopus 로고    scopus 로고
    • Seeding of a beta fibril formation is inhibited by all three isotypes of apolipoprotein E
    • Wood S. J., Chan W., and Wetzel R. (1996a) Seeding of A beta fibril formation is inhibited by all three isotypes of apolipoprotein E. Biochemistry 35, 12623-12628.
    • (1996) Biochemistry , vol.35 , pp. 12623-12628
    • Wood, S.J.1    Chan, W.2    Wetzel, R.3
  • 74
    • 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., Maleef B., Hart T., and Wetzel R. (1996b) 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    Maleef, B.2    Hart, T.3    Wetzel, R.4
  • 75
    • 0026686938 scopus 로고
    • Commentary and perspective on studies of beta amyloid neurotoxicity
    • Yankner B. A. (1992) Commentary and perspective on studies of beta amyloid neurotoxicity. Neurobiol. Aging 13, 615-616.
    • (1992) Neurobiol. Aging , vol.13 , pp. 615-616
    • Yankner, B.A.1
  • 76
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B. A., Duffy L. K., and Kirschner D. A. (1990) Neurotrophic and neurotoxic effects of amyloid beta 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.