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Volumn 24, Issue 3, 2003, Pages 415-420

Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1-42) in a transgenic Caenorhabditis elegans model

Author keywords

Alzheimer's disease; Amyloid beta peptide; Caenorhabditis elegans; Oxidative stress; Protein oxidation; Senile plaque

Indexed keywords

AMYLOID BETA PROTEIN; CARBONYL DERIVATIVE;

EID: 12244281810     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-4580(02)00225-7     Document Type: Article
Times cited : (329)

References (51)
  • 1
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of beta-amyloid peptide A beta (1-40) neurotoxicity accompanied by abrogation of fibril formation and A beta fragmentation
    • Aksenov M.Y., Aksenova M.V., Butterfield D.A., Hensley K., Vigo-Pelfrey C., Carney J.M. Glutamine synthetase-induced enhancement of beta-amyloid peptide A beta (1-40) neurotoxicity accompanied by abrogation of fibril formation and A beta fragmentation. J. Neurochem. 66:1996;2050-2056.
    • (1996) J. Neurochem. , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 2
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada P.V., Growdon J.H., Hedley-Whyte E.T., Hyman B.T. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology. 42:1992;631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 4
    • 0028207907 scopus 로고
    • Amyloid beta peptide induces necrosis rather than apoptosis
    • Behl C., Davis J.B., Klier F.G., Schubert D. Amyloid beta peptide induces necrosis rather than apoptosis. Brain Res. 645:1994;253-264.
    • (1994) Brain Res. , vol.645 , pp. 253-264
    • Behl, C.1    Davis, J.B.2    Klier, F.G.3    Schubert, D.4
  • 5
    • 0029967367 scopus 로고    scopus 로고
    • Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis
    • Braak H., Braak E. Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis. Acta Neuropathol. (Berlin). 92:1996;197-201.
    • (1996) Acta Neuropathol. (Berlin) , vol.92 , pp. 197-201
    • Braak, H.1    Braak, E.2
  • 7
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • Butterfield D.A., Drake J., Pocernich C., Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 7:2001;548-554.
    • (2001) Trends Mol. Med. , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 8
    • 0035997233 scopus 로고    scopus 로고
    • Review: Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid β-peptide 1-42
    • Butterfield D.A., Kanski J. Review: methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid β-peptide 1-42. Peptides. 23:2002;1299-1309.
    • (2002) Peptides , vol.23 , pp. 1299-1309
    • Butterfield, D.A.1    Kanski, J.2
  • 9
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress(1,2)
    • Butterfield D.A., Lauderback C.M. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress(1,2). Free Radic. Biol. Med. 32:2002;1050-1060.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 11
    • 0030710114 scopus 로고    scopus 로고
    • The 'amyloid cascade hypothesis': Decoy or real McCoy? of AD
    • Davis J.N. 2nd, Chisholm J.C. The 'amyloid cascade hypothesis': decoy or real McCoy? of AD. Trends Neurosci. 20:1997;558-559.
    • (1997) Trends Neurosci. , vol.20 , pp. 558-559
    • Davis II, J.N.1    Chisholm, J.C.2
  • 12
    • 0031712488 scopus 로고    scopus 로고
    • In vivo aggregation of beta-amyloid peptide variants
    • Fay D.S., Fluet A., Johnson C.J., Link C.D. In vivo aggregation of beta-amyloid peptide variants. J. Neurochem. 71:1998;1616-1625.
    • (1998) J. Neurochem. , vol.71 , pp. 1616-1625
    • Fay, D.S.1    Fluet, A.2    Johnson, C.J.3    Link, C.D.4
  • 13
    • 0034718206 scopus 로고    scopus 로고
    • Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization
    • Findeis M.A. Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization. Biochim. Biophys. Acta. 1502:2000;76-84.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 76-84
    • Findeis, M.A.1
  • 15
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S., Lansbury P.T. Jr. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol. 2:2000;E115-19.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 115-119
    • Goldberg, M.S.1    Lansbury P.T., Jr.2
  • 16
    • 0031555397 scopus 로고    scopus 로고
    • Low concentrations of estradiol reduce beta-amyloid (25-35)-induced toxicity, lipid peroxidation and glucose utilization in human SK-N-SH neuroblastoma cells
    • Gridley K.E., Green P.S., Simpkins J.W. Low concentrations of estradiol reduce beta-amyloid (25-35)-induced toxicity, lipid peroxidation and glucose utilization in human SK-N-SH neuroblastoma cells. Brain Res. 778:1997;158-165.
    • (1997) Brain Res. , vol.778 , pp. 158-165
    • Gridley, K.E.1    Green, P.S.2    Simpkins, J.W.3
  • 17
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20:1997;154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 18
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by theAlzheimer's beta-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris M.E., Hensley K., Butterfield D.A., Leedle R.A., Carney J.M. Direct evidence of oxidative injury produced by theAlzheimer's beta-amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 131:1995;193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 19
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta-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. The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry. 32:1993;4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury P.T., Jr.3
  • 20
    • 0036087081 scopus 로고    scopus 로고
    • The hydrophobic environment of Met35 of Alzheimer's Aβ(1-42) is important for the neurotoxic and oxidative properties of the peptide
    • Kanski J., Aksenova M., Butterfield D.A. The hydrophobic environment of Met35 of Alzheimer's Aβ(1-42) is important for the neurotoxic and oxidative properties of the peptide. Neurotox. Res. 4:2002;219-223.
    • (2002) Neurotox. Res. , vol.4 , pp. 219-223
    • Kanski, J.1    Aksenova, M.2    Butterfield, D.A.3
  • 21
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide (1-42)
    • Kanski J., Aksenova M., Schoneich C., Butterfield D.A. Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide (1-42). Free Radic. Biol. Med. 32:2002;1205-1211.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1205-1211
    • Kanski, J.1    Aksenova, M.2    Schoneich, C.3    Butterfield, D.A.4
  • 22
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman R., Saitoh T. Advances in Alzheimer's disease. FASEB J. 5:1991;278-286.
    • (1991) FASEB J. , vol.5 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 23
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • Keller J.N., Pang Z., Geddes J.W., Begley J.G., Germeyer A., Waeg G.et al. Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: role of the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 69:1997;273-284.
    • (1997) J. Neurochem. , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3    Begley, J.G.4    Germeyer, A.5    Waeg, G.6
  • 25
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury P.T. Jr. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U.S.A. 96:1999;3342-3344.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3342-3344
    • Lansbury P.T., Jr.1
  • 27
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • Link C.D. Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 92:1995;9368-9372.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 28
    • 0035109444 scopus 로고    scopus 로고
    • Visualization of fibrillar amyloid deposits in living, transgenic Caenorhabditis elegans animals using the sensitive amyloid dye X-34
    • Link C.D., Johnson C.J., Fonte V., Paupard M., Hall D.H., Styren S.et al. Visualization of fibrillar amyloid deposits in living, transgenic Caenorhabditis elegans animals using the sensitive amyloid dye X-34. Neurobiol. Aging. 22:2001;217-226.
    • (2001) Neurobiol. Aging , vol.22 , pp. 217-226
    • Link, C.D.1    Johnson, C.J.2    Fonte, V.3    Paupard, M.4    Hall, D.H.5    Styren, S.6
  • 30
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U.S.A. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 31
    • 0035500594 scopus 로고    scopus 로고
    • Stop making non-sense: The C. elegans smg genes
    • Mango S.E. Stop making non-sense: the C. elegans smg genes. Trends Genet. 17:2001;646-653.
    • (2001) Trends Genet. , vol.17 , pp. 646-653
    • Mango, S.E.1
  • 32
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • Mark R.J., Lovell M.A., Markesbery W.R., Uchida K., Mattson M.P. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide. J. Neurochem. 68:1997;255-264.
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 33
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23:1997;134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 35
    • 0028828044 scopus 로고
    • Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress
    • Oda T., Wals P., Osterburg H.H., Johnson S.A., Pasinetti G.M., Morgan T.E.et al. Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress. Exp. Neurol. 136:1995;22-31.
    • (1995) Exp. Neurol. , vol.136 , pp. 22-31
    • Oda, T.1    Wals, P.2    Osterburg, H.H.3    Johnson, S.A.4    Pasinetti, G.M.5    Morgan, T.E.6
  • 36
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike C.J., Walencewicz-Wasserman A.J., Kosmoski J., Cribbs D.H., Glabe C.G., Cotman C.W. Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J. Neurochem. 64:1995;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
  • 37
    • 0027936838 scopus 로고
    • Apolipoprotein E affects the rate of Alzheimer disease expression: Beta-amyloid burden is a secondary consequence dependent on APOE genotype and duration of disease
    • Roses A.D. Apolipoprotein E affects the rate of Alzheimer disease expression: beta-amyloid burden is a secondary consequence dependent on APOE genotype and duration of disease. J. Neuropathol. Exp. Neurol. 53:1994;429-437.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 429-437
    • Roses, A.D.1
  • 38
    • 0028132966 scopus 로고
    • Clinical correlates of cortical and nucleus basalis pathology in Alzheimer dementia
    • Samuel W., Terry R.D., DeTeresa R., Butters N., Masliah E. Clinical correlates of cortical and nucleus basalis pathology in Alzheimer dementia. Arch. Neurol. 51:1994;772-778.
    • (1994) Arch. Neurol. , vol.51 , pp. 772-778
    • Samuel, W.1    Terry, R.D.2    DeTeresa, R.3    Butters, N.4    Masliah, E.5
  • 39
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D., Barbour R., Dunn W., Gordon G., Grajeda H., Guido T.et al. Immunization with amyloid beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature. 400:1999;173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 40
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D., Eckman C., Jensen M., Song X., Citron M., Suzuki N.et al. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2:1996;864-870.
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6
  • 41
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 42
    • 0028168336 scopus 로고
    • Amyloid beta aggregation: Selective inhibition of aggregation in mixtures of amyloid with different chain lengths
    • Snyder S.W., Ladror U.S., Wade W.S., Wang G.T., Barrett L.W., Matayoshi E.D.et al. Amyloid beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J. 67:1994;1216-1228.
    • (1994) Biophys. J. , vol.67 , pp. 1216-1228
    • Snyder, S.W.1    Ladror, U.S.2    Wade, W.S.3    Wang, G.T.4    Barrett, L.W.5    Matayoshi, E.D.6
  • 43
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki N., Cheung T.T., Cai X.D., Odaka A., Otvos L. Jr., Eckman C.et al. An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science. 264:1994;1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos L., Jr.5    Eckman, C.6
  • 44
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry R.D., Masliah E., Salmon D.P., Butters N., DeTeresa R., Hill R.et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30:1991;572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6
  • 45
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35). J. Am. Chem. Soc. 123:2001;5625-5631.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 46
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J. Struct. Biol. 130:2000;184-208.
    • (2000) J. Struct. Biol. , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 47
    • 23044520785 scopus 로고    scopus 로고
    • Alzheimer's amyloid β peptide (1-42) fibrils are not always neurotoxic
    • Varadarajan S., Yatin S., Butterfield D.A. Alzheimer's amyloid β peptide (1-42) fibrils are not always neurotoxic. Alz. Rep. 3:2000;71-76.
    • (2000) Alz. Rep. , vol.3 , pp. 71-76
    • Varadarajan, S.1    Yatin, S.2    Butterfield, D.A.3
  • 48
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A.et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274:1999;45-52.
    • (1999) J. Biol. Chem. , vol.274 , pp. 45-52
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 49
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S.et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:2002;535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 50
    • 0033788416 scopus 로고    scopus 로고
    • Vitamin E prevents Alzheimer's amyloid β-peptide (1-42)-induced neuronal protein oxidation and reactive oxygen species production
    • Yatin S., Varadarajan S., Butterfield D.A. Vitamin E prevents Alzheimer's amyloid β-peptide (1-42)-induced neuronal protein oxidation and reactive oxygen species production. J. Alz. Dis. 2:2000;123-131.
    • (2000) J. Alz. Dis. , vol.2 , pp. 123-131
    • Yatin, S.1    Varadarajan, S.2    Butterfield, D.A.3
  • 51
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42)
    • Yatin S.M., Varadarajan S., Link C.D., Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42). Neurobiol. Aging. 20:1999;325-330.
    • (1999) Neurobiol. Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4


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