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Volumn 66, Issue 2, 1996, Pages 723-732

Zinc-induced aggregation of human and rat β-amyloid peptides in vitro

Author keywords

Aggregation; Alzheimer's disease; Zinc; Amyloid

Indexed keywords

AMYLOID BETA PROTEIN; ZINC;

EID: 0030066143     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66020723.x     Document Type: Article
Times cited : (127)

References (63)
  • 1
    • 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
    • Assafe, S.Y.1    Chung, S.-H.2
  • 2
    • 0040113568 scopus 로고
    • Amino acid analysis of peptides
    • (Gross E. and Meienhofer J., eds), Academic Press, New York
    • Benson J. R., Louie P. C., and Bradshaw R. A. (1981) Amino acid analysis of peptides, in The Peptides, Vol 4 (Gross E. and Meienhofer J., eds), pp. 217-260. Academic Press, New York.
    • (1981) The Peptides, Vol 4 , vol.4 , pp. 217-260
    • Benson, J.R.1    Louie, P.C.2    Bradshaw, R.A.3
  • 5
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio J., Lorenzo A., and Yankner B. A. (1992) Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging 13, 609-612.
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 6
    • 0027407570 scopus 로고
    • Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D. H., Matsudaira P., and Yankner B. A. (1993) Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA. 90, 2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 7
    • 0028180196 scopus 로고
    • Modulation of Aβ adhesiveness and secretase site cleavage by zinc
    • Bush A. I., Pettingell W. H., d. Paradis M., and Tanzi R. E. (1994a) Modulation of Aβ adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269, 12152-12158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell, W.H.2    D. Paradis, M.3    Tanzi, R.E.4
  • 9
  • 10
    • 0022878817 scopus 로고
    • In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein
    • Castaño E. M., Ghiso J., Prelli F., Gorevic P. D., Migheli A., and Frangione B. (1986) In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease β-protein. Biochem. Biophys. Res. Commun. 141, 782-789.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 782-789
    • Castaño, E.M.1    Ghiso, J.2    Prelli, F.3    Gorevic, P.D.4    Migheli, A.5    Frangione, B.6
  • 12
    • 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., and 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
  • 13
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor J. R., Menzies S. L., Martin S., and Mufson E. J. ( 1992) A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J. Neurosci. Res. 31, 75-83.
    • (1992) J. Neurosci. Res. , vol.31 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    Martin, S.3    Mufson, E.J.4
  • 14
    • 13344272118 scopus 로고
    • Spectroscopy
    • (Bull A. T., ed), Longmans, London
    • d'Albis A. and Gratzer W. B. (1970) Spectroscopy, in Companion to Biochemistry (Bull A. T., ed), p. 175. Longmans, London.
    • (1970) Companion to Biochemistry , pp. 175
    • D'Albis, A.1    Gratzer, W.B.2
  • 15
    • 0014280724 scopus 로고
    • Measurements of plasma zinc. I. In health and disease
    • Davies I. J. T., Musa M., and Dormandy T. L. (1968) Measurements of plasma zinc. I. In health and disease. J. Clin. Pathol. 21, 359-363.
    • (1968) J. Clin. Pathol. , vol.21 , pp. 359-363
    • Davies, I.J.T.1    Musa, M.2    Dormandy, T.L.3
  • 17
    • 0026605345 scopus 로고
    • Zinc, a neurotoxin to cultured neurons, contaminates cycad flour prepared by traditional Guamanian methods
    • Duncan M. W., Marini A. M., Watters R., Kopin I. J., and Markey S. P. (1992) Zinc, a neurotoxin to cultured neurons, contaminates cycad flour prepared by traditional Guamanian methods. J. Neurosci. 12, 1523-1537.
    • (1992) J. Neurosci. , vol.12 , pp. 1523-1537
    • Duncan, M.W.1    Marini, A.M.2    Watters, R.3    Kopin, I.J.4    Markey, S.P.5
  • 18
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer's disease
    • Evans K. C., Berger E. P., Cho C.-G., Weisgraber K. H., and Lansbury P. T. Jr. (1995) Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 92, 763-767.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.-G.3    Weisgraber, K.H.4    Lansbury Jr., P.T.5
  • 20
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser P. E., Nguyen J. T., Chin D. T., and Kirschner D. A. (1992) Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J. Neurochem. 59, 1531-1540.
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 22
    • 0028181486 scopus 로고
    • Alzheimer Aβ amyloid forms an inhibitory neuronal substrate
    • Fraser P. E., Lévesque L., and McLachlan D. R. (1994) Alzheimer Aβ amyloid forms an inhibitory neuronal substrate. J. Neurochem. 62, 1227-1230.
    • (1994) J. Neurochem. , vol.62 , pp. 1227-1230
    • Fraser, P.E.1    Lévesque, L.2    McLachlan, D.R.3
  • 23
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson C. J. (1989) Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol. 31, 145-238.
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 24
    • 0020502042 scopus 로고
    • Cytoarchitectonic distribution of zinc in the hippocampus of man and the rat
    • Frederickson C. J., Klitenick M. A., Manton W. I., and Kirkpatrick J. B. (1983) Cytoarchitectonic distribution of zinc in the hippocampus of man and the rat. Brain Res. 273, 335-339.
    • (1983) Brain Res. , vol.273 , pp. 335-339
    • Frederickson, C.J.1    Klitenick, M.A.2    Manton, W.I.3    Kirkpatrick, J.B.4
  • 25
    • 0011209984 scopus 로고
    • Imaging of calcium and aluminum in neurofibrillary tangle-bearing neurons in parkinsonism-dementia of Guam
    • Garruto R. M., Fukatsu R., Yanagihara R. T., Gajdusek D. C., Hook G., and Fiori C. E. (1984) Imaging of calcium and aluminum in neurofibrillary tangle-bearing neurons in parkinsonism-dementia of Guam. Proc. Natl. Acad. Sci USA 81, 1875-1879.
    • (1984) Proc. Natl. Acad. Sci USA , vol.81 , pp. 1875-1879
    • Garruto, R.M.1    Fukatsu, R.2    Yanagihara, R.T.3    Gajdusek, D.C.4    Hook, G.5    Fiori, C.E.6
  • 26
    • 0021207461 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. 122, 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 27
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgeber D., Lerman J. I., McBride O. W., Saffioti U., and Gajdusek D. C. (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235, 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgeber, D.1    Lerman, J.I.2    McBride, O.W.3    Saffioti, U.4    Gajdusek, D.C.5
  • 29
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • Halverson K., Fraser P. E., Kirschner D. A., and Lansbury P. T. Jr. (1990) Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry 29, 2639-2644.
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury Jr., P.T.4
  • 30
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J. and Allsop D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 31
    • 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 W. 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, W.H.6
  • 32
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich C., Kisters-Woike B., Reed J., Masters C. L., and Beyreuther K. (1991) Aggregation and secondary structure of synthetic amyloid βA4 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
  • 33
    • 0022535539 scopus 로고
    • Perforant pathway changes and memory impairment of Alzheimer's disease
    • Hyman B. T., Van Hoesen G. W., Kroner L. J., and Damasio A. R. (1986) Perforant pathway changes and memory impairment of Alzheimer's disease. Ann. Neurol. 20, 472-481.
    • (1986) Ann. Neurol. , vol.20 , pp. 472-481
    • Hyman, B.T.1    Van Hoesen, G.W.2    Kroner, L.J.3    Damasio, A.R.4
  • 34
    • 84996402700 scopus 로고
    • Ultraviolet absorption spectra of poly-L-glutamic acid
    • Imahori K. and Tanaka J. (1959) Ultraviolet absorption spectra of poly-L-glutamic acid. J. Mol. Biol. 1, 359-364.
    • (1959) J. Mol. Biol. , vol.1 , pp. 359-364
    • Imahori, K.1    Tanaka, J.2
  • 35
    • 0026631036 scopus 로고
    • The seminal role of β-amyloid in the pathogenesis of Alzheimer disease
    • Joachim C. L. and Selkoe D. J. (1992) The seminal role of β-amyloid in the pathogenesis of Alzheimer disease. Alzheimer Dis. Assoc. Disord. 6, 7-34.
    • (1992) Alzheimer Dis. Assoc. Disord. , vol.6 , pp. 7-34
    • Joachim, C.L.1    Selkoe, D.J.2
  • 37
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to β protein from Alzheimer's disease forms amyloid-like fibrils in vitro
    • Kirschner D. A., Inouye H., Duffy L. K., Sinclair A., Lind M, and Selkoe D. J. (1987) Synthetic peptide homologous to β protein from Alzheimer's disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA 84, 6953-6957.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6953-6957
    • Kirschner, D.A.1    Inouye, H.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 38
    • 0026646328 scopus 로고
    • In vivo neurotoxicity of β-amyloid [β(1-40)] and the β(25-35) fragment
    • Kowall N. W., McKee A. C., Yankner B. A., and Beal M. F. (1992) In vivo neurotoxicity of β-amyloid [β(1-40)] and the β(25-35) fragment. Neurobiol. Aging 13, 537-542.
    • (1992) Neurobiol. Aging , vol.13 , pp. 537-542
    • Kowall, N.W.1    McKee, A.C.2    Yankner, B.A.3    Beal, M.F.4
  • 42
    • 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. E. (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.E.7
  • 43
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M. P., Cheng B., Davis D., Bryant K., Leiberburg I., and Rydel R. (1992) β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Leiberburg, I.5    Rydel, R.6
  • 44
    • 0020000591 scopus 로고
    • Intraneuronal aluminum accumulation in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam
    • Perl D. P., Gajdusek D. C., Garruto R. M., Yanagihara R. T., and Gibbs C. J. (1982) Intraneuronal aluminum accumulation in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam. Science 217, 1053-1055.
    • (1982) Science , vol.217 , pp. 1053-1055
    • Perl, D.P.1    Gajdusek, D.C.2    Garruto, R.M.3    Yanagihara, R.T.4    Gibbs, C.J.5
  • 45
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures
    • Pike C. J., Walencewicz J., Glabe C. G., and Cotman C. W. (1991a) Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207, 367-368.
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, J.2    Glabe, C.G.3    Cotman, C.W.4
  • 46
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike C. J., Walencewicz J., Glabe C. G., and Cotman C. W. (1991b) 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, J.2    Glabe, C.G.3    Cotman, C.W.4
  • 47
    • 0026671781 scopus 로고
    • β-Amyloid induces neuritic dystrophy in vitro: Similarities with Alzheimer pathology
    • Pike C. J., Cummings B. J., and Cotman C. W. (1992) β-Amyloid induces neuritic dystrophy in vitro: similarities with Alzheimer pathology. Neuroreport 3, 769-772.
    • (1992) Neuroreport , vol.3 , pp. 769-772
    • Pike, C.J.1    Cummings, B.J.2    Cotman, C.W.3
  • 48
    • 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., and 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
  • 49
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike C. J., Walencewicz-Wasserman A. J., Kosmoski J., Cribbs D. H., Glabe C. G., and Cotman C W. (1995) Structure-activity analyses of β-amyloid peptides: contributions of the β25-35 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
  • 50
    • 0003882801 scopus 로고
    • IRL Press at Oxford University Press, Oxford
    • Roberts G. C. K. (1993) NMR of Macromolecules, pp. 15-16. IRL Press at Oxford University Press, Oxford.
    • (1993) NMR of Macromolecules , pp. 15-16
    • Roberts, G.C.K.1
  • 51
    • 0026065197 scopus 로고
    • β-Amyloid from Alzheimer disease brains inhibits sprouting and survival of sympathetic neurons
    • Roher A. E., Ball M. I., Bhave S. V., and Wakade A. R. (1991) β-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.I.2    Bhave, S.V.3    Wakade, A.R.4
  • 52
    • 73049144001 scopus 로고
    • The far ultraviolet absorption spectra of polypeptide and protein solutions and their depen-dence on conformation
    • Rosenheck K. and Doty P. (1961) The far ultraviolet absorption spectra of polypeptide and protein solutions and their depen-dence on conformation. Proc. Natl. Acad. Sci. USA 47, 1775-1789.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1775-1789
    • Rosenheck, K.1    Doty, P.2
  • 53
    • 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
  • 54
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe D. J. (1994) Alzheimer's disease: a central role for amyloid. J. Neuropathol. Exp. Neurol. 53, 438-447.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 57
    • 0023850791 scopus 로고
    • Protease inhibitor domain encoded by an amyloid precursor protein mRNA associated with Alzheimer's disease
    • Tanzi R. E., McClatchey A. I , Lamperti E. D., Villa-Komaroff L. L., Gusella J. F., and Neve R. L. (1987) Protease inhibitor domain encoded by an amyloid precursor protein mRNA associated with Alzheimer's disease. Nature 331, 528-530.
    • (1987) Nature , vol.331 , pp. 528-530
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.L.4    Gusella, J.F.5    Neve, R.L.6
  • 58
    • 0026558595 scopus 로고
    • Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels
    • Tomaoka A., Kalaria R., Lieberburg I., and Selkoe D. (1992) Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels. Proc. Natl. Acad. Sci. USA 89, 1345-1349.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1345-1349
    • Tomaoka, A.1    Kalaria, R.2    Lieberburg, I.3    Selkoe, D.4
  • 59
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic β-amyloid peptide
    • Tomski S. J. and Murphy R. M. (1992) Kinetics of aggregation of synthetic β-amyloid peptide. Arch. Biochem. Biophys. 294, 630-638.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 630-638
    • Tomski, S.J.1    Murphy, R.M.2
  • 60
    • 0001457779 scopus 로고
    • Radioimmunoassay of tachykinins
    • Too H. P. and Maggio J. E. (1991) Radioimmunoassay of tachykinins. Methods Neurosci. 6, 232-247.
    • (1991) Methods Neurosci. , vol.6 , pp. 232-247
    • Too, H.P.1    Maggio, J.E.2
  • 61
    • 0028861225 scopus 로고
    • Concentrations of amyloid β-protein in cerebrospinal fluid of patients with Alzheimer's disease
    • van Gool W. A., Kuiper M. A., Walstra G. J. M., Wolters E. Ch, and Bolhuis P. A. (1994) Concentrations of amyloid β-protein in cerebrospinal fluid of patients with Alzheimer's disease. Ann. Neurol. 37, 277-279.
    • (1994) Ann. Neurol. , vol.37 , pp. 277-279
    • Van Gool, W.A.1    Kuiper, M.A.2    Walstra, G.J.M.3    Wolters, E.Ch.4    Bolhuis, P.A.5
  • 62
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer D. B. (1962) Ultraviolet spectra of proteins and amino acids. Adv. Protein Chem. 17, 304-405.
    • (1962) Adv. Protein Chem. , vol.17 , pp. 304-405
    • Wetlaufer, D.B.1
  • 63
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of β-protein: Reversal by tachykinin neuropeptides
    • Yankner B. A., Duffy L. K., and Kirschner D. A. (1990) Neurotrophic and neurotoxic effects of 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


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