메뉴 건너뛰기




Volumn 45, Issue 1, 2003, Pages 117-127

Involvement of oxidative stress in the enhancement of acetylcholinesterase activity induced by amyloid beta-peptide

Author keywords

Acetylcholinesterase; Beta amyloid; Nitric oxide synthase; Oxidative stress; Retinal cells

Indexed keywords

7 NITROINDAZOLE; ACETYLCHOLINE; ACETYLCHOLINESTERASE; ALPHA TOCOPHEROL; AMYLOID BETA PROTEIN; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE SYNTHASE INHIBITOR; REACTIVE OXYGEN METABOLITE;

EID: 0037219182     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(02)00201-8     Document Type: Article
Times cited : (239)

References (63)
  • 1
    • 0033614679 scopus 로고    scopus 로고
    • Both oxidative stress-dependent and independent effects of amyloid beta protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction assay
    • Abe K., Saito H. Both oxidative stress-dependent and independent effects of amyloid beta protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction assay. Brain Res. 830:1999;146-154.
    • (1999) Brain Res. , vol.830 , pp. 146-154
    • Abe, K.1    Saito, H.2
  • 6
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-β peptide fragments by forming a complex with growing fibrils
    • Alvarez A., Opazo C., Alarcón R., Garrido J., Inestrosa N.C. Acetylcholinesterase promotes the aggregation of amyloid-β peptide fragments by forming a complex with growing fibrils. J. Mol. Biol. 272:1997;348-361.
    • (1997) J. Mol. Biol. , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcón, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 7
    • 0020545113 scopus 로고
    • Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: Selective loss of the intermediate (10S) form
    • Atack J.R., Perry E.K., Bonham J.R., Perry R.H., Tomlinson B.E., Blessed G., Fairbairn A. Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: selective loss of the intermediate (10S) form. Neurosci. Lett. 40:1983;199-204.
    • (1983) Neurosci. Lett. , vol.40 , pp. 199-204
    • Atack, J.R.1    Perry, E.K.2    Bonham, J.R.3    Perry, R.H.4    Tomlinson, B.E.5    Blessed, G.6    Fairbairn, A.7
  • 9
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β-protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β-protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 10
    • 0000416021 scopus 로고
    • UV-assay with pyruvate and NADH
    • H.U. Bergmeyer. New York: Academic Press
    • Bergmeyer H.U., Brent E. UV-assay with pyruvate and NADH. Bergmeyer H.U. Methods of Enzymatic Analysis. 1974;574-579 Academic Press, New York.
    • (1974) Methods of Enzymatic Analysis , pp. 574-579
    • Bergmeyer, H.U.1    Brent, E.2
  • 11
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • Buege J.A., Aust S.D. Microsomal lipid peroxidation. Methods Enzymol. 52:1967;302-310.
    • (1967) Methods Enzymol. , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 12
    • 0032749577 scopus 로고    scopus 로고
    • The possible origin of free radicals from amyloid β-peptides in Alzheimer's disease
    • Bus A.I., Huang X., Fairlie D.P. The possible origin of free radicals from amyloid β-peptides in Alzheimer's disease. Neurobiol. Aging. 20:1999;335-337.
    • (1999) Neurobiol. Aging , vol.20 , pp. 335-337
    • Bus, A.I.1    Huang, X.2    Fairlie, D.P.3
  • 13
    • 0028178837 scopus 로고
    • β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D.A., Hensley K., Harris M., Mattson M., Carney J. β-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200:1994;710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.5
  • 15
    • 0033580128 scopus 로고    scopus 로고
    • Beta-amyloid levels predict cholinesterase activity in human cerebrospinal fluid
    • Carroll R.T., Lust M.R., Emmerling M.R. Beta-amyloid levels predict cholinesterase activity in human cerebrospinal fluid. Neuroreport. 10:1999;127-130.
    • (1999) Neuroreport , vol.10 , pp. 127-130
    • Carroll, R.T.1    Lust, M.R.2    Emmerling, M.R.3
  • 16
    • 0031980737 scopus 로고    scopus 로고
    • Calcium influx through AMPA receptors and through calcium channels is regulated by protein kinase C in cultured retina amacrine-like cells
    • Carvalho A.L., Duarte C.B., Faro C.J., Carvalho A.P., Pires E.V. Calcium influx through AMPA receptors and through calcium channels is regulated by protein kinase C in cultured retina amacrine-like cells. J. Neurochem. 70:1998;2112-2119.
    • (1998) J. Neurochem. , vol.70 , pp. 2112-2119
    • Carvalho, A.L.1    Duarte, C.B.2    Faro, C.J.3    Carvalho, A.P.4    Pires, E.V.5
  • 17
    • 0021027358 scopus 로고
    • Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay
    • Cathcart R., Schwiers E., Ames B.N. Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Anal. Biochem. 134:1983;111-116.
    • (1983) Anal. Biochem. , vol.134 , pp. 111-116
    • Cathcart, R.1    Schwiers, E.2    Ames, B.N.3
  • 20
    • 0034728670 scopus 로고    scopus 로고
    • β-Amyloid-induced calcium influx induces apoptosis in culture by oxidative stress rather than tau phosphorylation
    • Ekinci F.J., Linsley M.-D., Shea T.B. β-Amyloid-induced calcium influx induces apoptosis in culture by oxidative stress rather than tau phosphorylation. Mol. Brain Res. 76:2000;389-395.
    • (2000) Mol. Brain Res. , vol.76 , pp. 389-395
    • Ekinci, F.J.1    Linsley, M.-D.2    Shea, T.B.3
  • 21
    • 0033569760 scopus 로고    scopus 로고
    • Activation of the L voltage-sensitive calcium channel by mitogen-activated protein (MAP) kinase following exposure of neuronal cells to β-amyloid. MAP kinase mediates β-amyloid-induced neurodegeneration
    • Ekinci F.J., Malik K.M., Shea T.B. Activation of the L voltage-sensitive calcium channel by mitogen-activated protein (MAP) kinase following exposure of neuronal cells to β-amyloid. MAP kinase mediates β-amyloid-induced neurodegeneration. J. Biol. Chem. 274:1999;30322-30327.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30322-30327
    • Ekinci, F.J.1    Malik, K.M.2    Shea, T.B.3
  • 23
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Rad. Biol. Med. 11:1991;81-128.
    • (1991) Free Rad. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 24
    • 0029923244 scopus 로고    scopus 로고
    • Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein
    • Fraser S.P., Suh Y.-H., Chong Y.H., Djamgoz M.B.A. Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein. J. Neurochem. 66:1996;2034-2040.
    • (1996) J. Neurochem. , vol.66 , pp. 2034-2040
    • Fraser, S.P.1    Suh, Y.-H.2    Chong, Y.H.3    Djamgoz, M.B.A.4
  • 25
    • 0002037940 scopus 로고
    • Cholinergic systems and related neuropathological predilection patterns in Alzheimer disease
    • R.D. Terry, R. Katzman, & K.L. Bick. New York: Raven press
    • Geula C., Mesulam M.-M. Cholinergic systems and related neuropathological predilection patterns in Alzheimer disease. Terry R.D., Katzman R., Bick K.L. Alzheimer Disease. 1994;263-291 Raven press, New York.
    • (1994) Alzheimer Disease , pp. 263-291
    • Geula, C.1    Mesulam, M.-M.2
  • 26
    • 0029102993 scopus 로고
    • Neurodegeneration mediated by glutamate and β-amyloid peptide: A comparison and possible interaction
    • Gray C.W., Pattel A.J. Neurodegeneration mediated by glutamate and β-amyloid peptide: a comparison and possible interaction. Brain Res. 691:1995;169-179.
    • (1995) Brain Res. , vol.691 , pp. 169-179
    • Gray, C.W.1    Pattel, A.J.2
  • 27
    • 0032901459 scopus 로고    scopus 로고
    • N-methyl-D-Aspartate receptor antagonist MK-801 and radical scavengers protect cholinergic nucleus basalis neurons against β-amyloid neurotoxicity
    • Harkany T., Mulder J., Sasvári M., Ábrahám I., Kónya C., Zarándi M., Penke B., Luiten P.G.M., Nyakas C. N-methyl-D-Aspartate receptor antagonist MK-801 and radical scavengers protect cholinergic nucleus basalis neurons against β-amyloid neurotoxicity. Neurobiol. Dis. 6:1999;109-121.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 109-121
    • Harkany, T.1    Mulder, J.2    Sasvári, M.3    Ábrahám, I.4    Kónya, C.5    Zarándi, M.6    Penke, B.7    Luiten, P.G.M.8    Nyakas, C.9
  • 29
    • 0027490070 scopus 로고
    • The lack of accumulation of senile plaques or amyloid burden in Alzheimer's disease suggests a dynamic balance between amyloid deposition and resolution
    • Hyman B.T., Marzloff K., Arriagada P.V. The lack of accumulation of senile plaques or amyloid burden in Alzheimer's disease suggests a dynamic balance between amyloid deposition and resolution. J. Neuropathol. Exp. Neurol. 52:1993;594-600.
    • (1993) J. Neuropathol. Exp. Neurol. , vol.52 , pp. 594-600
    • Hyman, B.T.1    Marzloff, K.2    Arriagada, P.V.3
  • 30
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa N.C., Alvarez A., Pérez C.A., Moreno R.D., Vicente M., Linker C., Casanueva O.I., Soto C., Garrido J. Acetylcholinesterase accelerates assembly of amyloid β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron. 16:1996;881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 32
    • 0033621641 scopus 로고    scopus 로고
    • Human amyloid-β 1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat
    • Kasa P., Papp H., Kovacs I., Forgon M., Penke B., Yamaguchi H. Human amyloid-β 1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat. Neurosci. Lett. 278:2000;117-119.
    • (2000) Neurosci. Lett. , vol.278 , pp. 117-119
    • Kasa, P.1    Papp, H.2    Kovacs, I.3    Forgon, M.4    Penke, B.5    Yamaguchi, H.6
  • 33
    • 0030767243 scopus 로고    scopus 로고
    • The cholinergic system in Alzheimer's disease
    • Kasa P., Rakonczany Z., Gulya K. The cholinergic system in Alzheimer's disease. Prog. Neurobiol. 52:1997;511-535.
    • (1997) Prog. Neurobiol. , vol.52 , pp. 511-535
    • Kasa, P.1    Rakonczany, Z.2    Gulya, K.3
  • 35
    • 0034883504 scopus 로고    scopus 로고
    • Neuroprotective and neurorescuing effects of isoform-specific nitric oxide synthase inhibitors, nitric oxide scavenger, and antioxidant against beta-amyloid toxicity
    • Law A., Gauthier S., Quirion R. Neuroprotective and neurorescuing effects of isoform-specific nitric oxide synthase inhibitors, nitric oxide scavenger, and antioxidant against beta-amyloid toxicity. Br. J. Pharmacol. 133:2001;1114-1124.
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 1114-1124
    • Law, A.1    Gauthier, S.2    Quirion, R.3
  • 36
    • 0035105932 scopus 로고    scopus 로고
    • Say NO to Alzheimer's disease: The putative links between nitric oxide and dementia of the Alzheimer's type
    • Law A., Gauthier S., Quirion R. Say NO to Alzheimer's disease: the putative links between nitric oxide and dementia of the Alzheimer's type. Brain Res. Rev. 1:2001;73-96.
    • (2001) Brain Res. Rev. , vol.1 , pp. 73-96
    • Law, A.1    Gauthier, S.2    Quirion, R.3
  • 37
    • 0030695856 scopus 로고    scopus 로고
    • Cytotoxic amyloid peptides inhibit cellular3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis
    • Liu Y., Schubert D. Cytotoxic amyloid peptides inhibit cellular3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis. J Neurochem. 69:1997;2285-2293.
    • (1997) J Neurochem. , vol.69 , pp. 2285-2293
    • Liu, Y.1    Schubert, D.2
  • 38
    • 0035860603 scopus 로고    scopus 로고
    • Expression of endothelial and inducible NOS-isoforms is increased in Alzheimer's disease, in APP23 transgenic mice and after experimental brain lesion in rat: Evidence for an induction by amyloid pathology
    • Luth H., Holzer M., Gartner U., Staufenbiel M., Arendt T. Expression of endothelial and inducible NOS-isoforms is increased in Alzheimer's disease, in APP23 transgenic mice and after experimental brain lesion in rat: evidence for an induction by amyloid pathology. Brain Res. 913:2001;57-67.
    • (2001) Brain Res. , vol.913 , pp. 57-67
    • Luth, H.1    Holzer, M.2    Gartner, U.3    Staufenbiel, M.4    Arendt, T.5
  • 39
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hidroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide
    • Mark R.J., Lovell M.A., Markesberry W.R., Uchida K., Mattson M.P. A role for 4-hidroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide. J. Neurochem. 68:1997;255-264.
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesberry, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 40
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R.J., Pang Z., Geddes J.W., Uchida K., Mattson M.P. Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci. 17:1997;1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 41
    • 0032007328 scopus 로고    scopus 로고
    • Modification of ion homeostasis by lipid peroxidation: Roles in neuronal degeneration and adaptive plasticity
    • Mattson M.P. Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity. Trends Neurosci. 21:1998;53-57.
    • (1998) Trends Neurosci. , vol.21 , pp. 53-57
    • Mattson, M.P.1
  • 42
    • 0029175202 scopus 로고
    • Calcium, free radicals, and excitotoxic neuronal death in primary cell culture
    • Mattson M.P., Barger S.W., Begley J.G., Mark R.J. Calcium, free radicals, and excitotoxic neuronal death in primary cell culture. Methods Cell Biol. 46:1995;187-216.
    • (1995) Methods Cell Biol. , vol.46 , pp. 187-216
    • Mattson, M.P.1    Barger, S.W.2    Begley, J.G.3    Mark, R.J.4
  • 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., Lieberburg I., Rydel R.E. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12:1992;379-389.
    • (1992) J. Neurosci. , vol.12 , pp. 379-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 46
    • 0027514286 scopus 로고
    • Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains
    • Morán M.A., Mufson E.J., Gómez-Ramos P. Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains. Acta Neuropathol. 85:1993;362-369.
    • (1993) Acta Neuropathol. , vol.85 , pp. 362-369
    • Morán, M.A.1    Mufson, E.J.2    Gómez-Ramos, P.3
  • 47
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival. J. Immunol. Methods. 65:1983;55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 48
    • 0033022771 scopus 로고    scopus 로고
    • Involvement of oxidative stress on the impairment of energy metabolism induced by Aβ peptides on PC12 cells: Protection by antioxidants
    • Pereira C., Santos M.S., Oliveira C. Involvement of oxidative stress on the impairment of energy metabolism induced by Aβ peptides on PC12 cells: protection by antioxidants. Neurobiol. Dis. 6:1999;209-219.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 209-219
    • Pereira, C.1    Santos, M.S.2    Oliveira, C.3
  • 49
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of protein assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.J., Cotman C.W. Neurodegeneration induced by β-amyloid peptides in vitro: the role of protein assembly state. J. Neurosci. 13:1993;1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.J.4    Cotman, C.W.5
  • 50
    • 0019886584 scopus 로고
    • 1-[4-(trimethylamino)phenyl-6-phrnylhexa-1,3,5-triene: Synthesis, fluorescence properties, and use as a fluorescence probe of lipid bilayers
    • Prendergast F.G., Haugland R.P., Callahan P.J. 1-[4-(trimethylamino)phenyl-6-phrnylhexa-1,3,5-triene: synthesis, fluorescence properties, and use as a fluorescence probe of lipid bilayers. Biochemistry. 20:1981;7333-7338.
    • (1981) Biochemistry , vol.20 , pp. 7333-7338
    • Prendergast, F.G.1    Haugland, R.P.2    Callahan, P.J.3
  • 51
    • 0029081382 scopus 로고
    • Dual effect of lipid peroxidation on the membrane order of retinal cells in culture
    • Rego A.C., Oliveira C.R. Dual effect of lipid peroxidation on the membrane order of retinal cells in culture. Arch. Biochem. Biophys. 321:1995;127-136.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 127-136
    • Rego, A.C.1    Oliveira, C.R.2
  • 52
    • 0032479530 scopus 로고    scopus 로고
    • Influence of vitamin E succinate on retinal cell survival
    • Rego A.C., Santos M.S., Proença M.T., Oliveira C.R. Influence of vitamin E succinate on retinal cell survival. Toxicology. 128:1998;113-124.
    • (1998) Toxicology , vol.128 , pp. 113-124
    • Rego, A.C.1    Santos, M.S.2    Proença, M.T.3    Oliveira, C.R.4
  • 53
    • 0031595164 scopus 로고    scopus 로고
    • 3H]Acetylcholine release from cultured amacrine-like neurons by adenosine A1 receptors
    • 3H]Acetylcholine release from cultured amacrine-like neurons by adenosine A1 receptors. J. Neurochem. 71:1998;1086-1094.
    • (1998) J. Neurochem. , vol.71 , pp. 1086-1094
    • Santos, P.F.1    Santos, M.S.2    Carvalho, A.P.3    Duarte, C.B.4
  • 54
    • 1842375103 scopus 로고    scopus 로고
    • The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells
    • Sberna G., Saez-Valero J., Beyreuther K., Masters C.L., Small D.H. The amyloid beta-protein of Alzheimer's disease increases acetylcholinesterase expression by increasing intracellular calcium in embryonal carcinoma P19 cells. J. Neurochem. 69:1997;1177-1184.
    • (1997) J. Neurochem. , vol.69 , pp. 1177-1184
    • Sberna, G.1    Saez-Valero, J.2    Beyreuther, K.3    Masters, C.L.4    Small, D.H.5
  • 55
    • 0031754362 scopus 로고    scopus 로고
    • Acetylcholinesterase is increased in the brains of transgenic mice expressing the C-terminal fragment (CT100) of the beta-amyloid protein precursor of Alzheimer's disease
    • Sberna G., Saez-Valero J., Li Q.X., Czech C., Beyreuther K., Masters C.L., McLean C.A., Small D.H. Acetylcholinesterase is increased in the brains of transgenic mice expressing the C-terminal fragment (CT100) of the beta-amyloid protein precursor of Alzheimer's disease. J. Neurochem. 71:1998;723-731.
    • (1998) J. Neurochem. , vol.71 , pp. 723-731
    • Sberna, G.1    Saez-Valero, J.2    Li, Q.X.3    Czech, C.4    Beyreuther, K.5    Masters, C.L.6    McLean, C.A.7    Small, D.H.8
  • 56
    • 0017390556 scopus 로고
    • A rapid sensitive and versatile assay for protein using Coomassie Brilliant Blue G250
    • Sedmak J.J., Grossero S.E. A rapid sensitive and versatile assay for protein using Coomassie Brilliant Blue G250. Anal. Biochem. 79:1977;544-552.
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossero, S.E.2
  • 57
    • 0018225465 scopus 로고
    • Fluidity parameters of lipid regions determined by fluorescence polarization
    • Shinitzky M., Barenholz Y. Fluidity parameters of lipid regions determined by fluorescence polarization. Biochim. Biophys. Acta. 555:1978;367-394.
    • (1978) Biochim. Biophys. Acta , vol.555 , pp. 367-394
    • Shinitzky, M.1    Barenholz, Y.2
  • 58
    • 0023850791 scopus 로고
    • Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease
    • Tanzi R.E., McClatchey A.I., Lamperti E.D., Villa-Komaroff L.T., Gusella J.F., Neve R.L. Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature. 331:1988;528-530.
    • (1988) Nature , vol.331 , pp. 528-530
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.T.4    Gusella, J.F.5    Neve, R.L.6
  • 59
    • 0035375277 scopus 로고    scopus 로고
    • Amyloid β-peptide induces nitric oxide production in rat hippocampus: Association with cholinergic dysfunction and amelioration by inducible nitric oxide synthase inhibitors
    • 10.1096/fj.00-0719fje
    • Tran, M.H., Yamada, K., Olariu, A., Mizuno, M., Ren, X.H., Nabeshima, T., 2001. Amyloid β-peptide induces nitric oxide production in rat hippocampus: association with cholinergic dysfunction and amelioration by inducible nitric oxide synthase inhibitors. FASEB J. 10.1096/fj.00-0719fje.
    • (2001) FASEB J.
    • Tran, M.H.1    Yamada, K.2    Olariu, A.3    Mizuno, M.4    Ren, X.H.5    Nabeshima, T.6
  • 60
    • 0025000725 scopus 로고
    • Senile plaques: Staining for acetylcholinesterase and A4 protein: A comparative study in the hippocampus and entorhinal cortex
    • Ulrich J., Meier-Ruge W., Probst A., Meier E., Ipsen S. Senile plaques: staining for acetylcholinesterase and A4 protein: a comparative study in the hippocampus and entorhinal cortex. Acta Neuropathol. 80:1990;624-628.
    • (1990) Acta Neuropathol. , vol.80 , pp. 624-628
    • Ulrich, J.1    Meier-Ruge, W.2    Probst, A.3    Meier, E.4    Ipsen, S.5
  • 61
    • 0019886355 scopus 로고
    • Lipid structural order parameters (reciprocal of fluidity) in biomembranes derived from steady-state fluorescence polarization measurements
    • Van Blitterswijk W.J., Van Hoeven R.P., Van der Meer B.W. Lipid structural order parameters (reciprocal of fluidity) in biomembranes derived from steady-state fluorescence polarization measurements. Biochim. Biophys. Acta. 644:1981;323-332.
    • (1981) Biochim. Biophys. Acta , vol.644 , pp. 323-332
    • Van Blitterswijk, W.J.1    Van Hoeven, R.P.2    Van der Meer, B.W.3
  • 62
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 63
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AβP-channel-mediated cellular toxicity
    • Zhu Y.J., Lin H., Lal R. Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AβP-channel-mediated cellular toxicity. FASEB J. 14:2000;1244-1254.
    • (2000) FASEB J. , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.