메뉴 건너뛰기




Volumn 25, Issue 5, 2004, Pages 563-568

Alzheimer's amyloid β-peptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide

Author keywords

Amyloid; Methionine; Neurotoxicity; Oxidative stress; peptide

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; FREE RADICAL; LIPID; METHIONINE; OXYGEN; PEPTIDE;

EID: 1842519391     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2003.12.027     Document Type: Article
Times cited : (128)

References (50)
  • 1
    • 0034504243 scopus 로고    scopus 로고
    • Measurement of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction activity and la dehydrogenase release using MTT
    • Abe K., Matsuki N. Measurement of cellular 3-(4, 5-dimethylthiazol-2-yl)- 2, 5-diphenyltetrazolium bromide (MTT) reduction activity and la dehydrogenase release using MTT. Neurosci. Res. 38:2000;325-329
    • (2000) Neurosci. Res. , vol.38 , pp. 325-329
    • Abe, K.1    Matsuki, N.2
  • 2
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's (beta)-amyloid Is from lipid membrane by methionine oxidation
    • Barnham K.J., Ciccotosto G.D., Tickler A.K., Ali F.E., Smith D.G., Williams Lam Y.H., et al. Neurotoxic, redox-competent Alzheimer's (beta)-amyloid Is from lipid membrane by methionine oxidation. J. Biol. Chem. 278:2003;42959-42965
    • (2003) J. Biol. Chem. , vol.278 , pp. 42959-42965
    • Barnham, K.J.1    Ciccotosto, G.D.2    Tickler, A.K.3    Ali, F.E.4    Smith, D.G.5    Williams Lam, Y.H.6
  • 6
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role of amyloid β-peptide
    • Butterfield D.A., Drake J., Pocernich C., Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role of amyloid β-peptide. Trends Molec. Med. 7:2001;548-554
    • (2001) Trends Molec. Med. , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 7
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress
    • Butterfield D.A., Lauderback C.M. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress. 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
  • 8
    • 0036753272 scopus 로고    scopus 로고
    • Review: Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contributes to neuronal death
    • Butterfield D.A., Castegna A., Lauderback C.M., Drake J. Review: evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contributes to neuronal death. Neurobiol. Aging. 23:2002;655-664
    • (2002) Neurobiol. Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 9
    • 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
  • 10
    • 0141767139 scopus 로고    scopus 로고
    • Proteomics in Alzheimer's disease: Insights into mechanisms of neurodegeneration
    • Butterfield D.A., Boyd-Kimball D., Castegna A. Proteomics in Alzheimer's disease: insights into mechanisms of neurodegeneration. J Neurochem. 86:2003;1313-1327
    • (2003) J Neurochem , vol.86 , pp. 1313-1327
    • Butterfield, D.A.1    Boyd-Kimball, D.2    Castegna, A.3
  • 11
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med. 33:2002;562-571
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6
  • 12
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II. Dihydropyrimidinase-related protein 2, α-enolase, and heat shock cognate 71
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II. Dihydropyrimidinase-related protein 2, α-enolase, and heat shock cognate 71. J. Neurochem. 82:2002;1524-1532
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6
  • 14
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide(1-40) in a water-micelle environment Is the membrane-spanning domain where we think it is?
    • Coles M., Bicknell W., Watson A.A., Fairlie D.P., Craik D.J. Solution structure of amyloid β-peptide(1-40) in a water-micelle environment Is the membrane-spanning domain where we think it is? Biochemistry. 37:1998;11064-11077
    • (1998) Biochemistry , vol.37 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, A.A.3    Fairlie, D.P.4    Craik, D.J.5
  • 15
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., Beyrether K., et al. Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276:2001;20466-20473
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyrether, K.6
  • 16
    • 0037775776 scopus 로고    scopus 로고
    • Selectively reduced expression of synaptic plasticity-related genes in amyloid precursor + presenilin-1 transgenic mice
    • Dickey C.A., Loring J.F., Montgomery J., Gordon M.N., Eastman P.S., Morgan D. Selectively reduced expression of synaptic plasticity-related genes in amyloid precursor + presenilin-1 transgenic mice. J. Neurosci. 23:2003;5219-5226
    • (2003) J. Neurosci. , vol.23 , pp. 5219-5226
    • Dickey, C.A.1    Loring, J.F.2    Montgomery, J.3    Gordon, M.N.4    Eastman, P.S.5    Morgan, D.6
  • 17
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong J., Atwood C.S., Anderson V.E., Siedlak S.L., Smith M.A., Perry G., et al. Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry. 42:2003;2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6
  • 18
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1-42) in a transgenic Caenorhabditis elegans model
    • Drake J., Link C.D., Butterfield D.A. Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1-42) in a transgenic Caenorhabditis elegans model. Neurobiol. Aging. 24:2003;415-420
    • (2003) Neurobiol. Aging , vol.24 , pp. 415-420
    • Drake, J.1    Link, C.D.2    Butterfield, D.A.3
  • 19
    • 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
  • 20
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita S.P., Aksenov M.Y., Lovell M.A., Markesbery W.R. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 73:1999;1660-1666
    • (1999) J. Neurochem. , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 21
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y., Chang L., Viola K.L., Lacor P.N., Lambert M.P., Finch C.E., et al. Alzheimer's disease-affected brain: presence of oligomeric aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. USA. 100:2003;10417-10422
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 22
    • 0028807137 scopus 로고
    • Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation
    • Hensley K., Hall N., Subramaniam R., Cole P., Harris M., Aksenov M., et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J. Neurochem. 65:1995;2146-2156
    • (1995) J. Neurochem. , vol.65 , pp. 2146-2156
    • Hensley, K.1    Hall, N.2    Subramaniam, R.3    Cole, P.4    Harris, M.5    Aksenov, M.6
  • 23
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease
    • Hou L., Kang I., Marchant R.E., Zagorski M.G. Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 277:2002;40173-40176
    • (2002) J. Biol. Chem. , vol.277 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 24
    • 18344414746 scopus 로고    scopus 로고
    • The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang X., Atwood C.S., Hartshorn M.A., Multhaup G., Goldstein L.E., Scarpa R.C., et al. The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry. 38:1999;7609-7616
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3    Multhaup, G.4    Goldstein, L.E.5    Scarpa, R.C.6
  • 25
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid β-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 β-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
  • 26
    • 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
  • 27
    • 0035918312 scopus 로고    scopus 로고
    • Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains
    • Kuo Y.W., Kokjohn T.A., Beach T.G., Sue L.I., Brune D., Lopez J.C., et al. Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains. J. Biol. Chem. 276:2001;12991-12998
    • (2001) J. Biol. Chem. , vol.276 , pp. 12991-12998
    • Kuo, Y.W.1    Kokjohn, T.A.2    Beach, T.G.3    Sue, L.I.4    Brune, D.5    Lopez, J.C.6
  • 28
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA. 95:1998;6448-6453
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 29
    • 0034925118 scopus 로고    scopus 로고
    • The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: Role of Aβ1-42
    • Lauderback C.M., Hackett J.M., Huang F.F., Keller J.N., Szweda L.I., Markesbery W.R., et al. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: role of Aβ1-42. J. Neurochem. 78:2001;413-416
    • (2001) J. Neurochem. , vol.78 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3    Keller, J.N.4    Szweda, L.I.5    Markesbery, W.R.6
  • 30
    • 0037016321 scopus 로고    scopus 로고
    • Apolipoprotein e modulates Alzheimer's Aβ(1-42)-induced oxidative damage to synaptosomes in an allele-specific manner
    • Lauderback C.M., Kanski J., Hackett J.M., Maeda N., Kindy M.S., Butterfield D.A. Apolipoprotein E modulates Alzheimer's Aβ(1-42)-induced oxidative damage to synaptosomes in an allele-specific manner. Brain Res. 924:2002;90-97
    • (2002) Brain Res. , vol.924 , pp. 90-97
    • Lauderback, C.M.1    Kanski, J.2    Hackett, J.M.3    Maeda, N.4    Kindy, M.S.5    Butterfield, D.A.6
  • 31
    • 0037345672 scopus 로고    scopus 로고
    • Expanding the association between the APOE gene and the risk of Alzheimer's disease: Possible roles for APOE promoter polymorphisms and alterations in APOE transcription
    • Laws S.M., Hone E., Gandy S., Martins R.N. Expanding the association between the APOE gene and the risk of Alzheimer's disease: possible roles for APOE promoter polymorphisms and alterations in APOE transcription. J. Neurochem. 84:2003;1215-1236
    • (2003) J. Neurochem. , vol.84 , pp. 1215-1236
    • Laws, S.M.1    Hone, E.2    Gandy, S.3    Martins, R.N.4
  • 32
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • Lovell M.A., Xie C., Markesbery W.R. Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures. Neurobiol. Aging. 22:2001;187-194
    • (2001) Neurobiol. Aging , vol.22 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 33
    • 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 β-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 β-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
  • 34
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer disease. Free Radic. Biol. Med. 23:1997;134-147
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 35
    • 0031980065 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery W.R., Lovell M.A. 4-Hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol. Aging. 19:1998;33-36
    • (1998) Neurobiol. Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 36
    • 0029811226 scopus 로고    scopus 로고
    • Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease
    • Masliah E., Alford M., DeTeresa R., Mallory M., Hansen L. Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease. Ann. Neurol. 40:1996;759-766
    • (1996) Ann. Neurol. , vol.40 , pp. 759-766
    • Masliah, E.1    Alford, M.2    Deteresa, R.3    Mallory, M.4    Hansen, L.5
  • 38
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid beta-peptide 1-40 oligomers
    • Palmblad M., Westlind-Danielsson A., Bergquist J. Oxidation of methionine 35 attenuates formation of amyloid beta-peptide 1-40 oligomers. J. Biol. Chem. 277:2002;19506-19510
    • (2002) J. Biol. Chem. , vol.277 , pp. 19506-19510
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 39
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modeling study
    • Pogocki D., Schoneich C. Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modeling study. Chem. Res. Toxicol. 15:2002;408-418
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 40
    • 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
  • 41
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease
    • Shao H., Jao S.C., Ma K., Zagorski M.G. Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease. J. Mol. Biol. 285:1999;755-773
    • (1999) J. Mol. Biol. , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.C.2    Ma, K.3    Zagorski, M.G.4
  • 42
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • Stadtman E.R., Moskovitz J., Berlett B.S., Levine R.L. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell Biochem. 234:2002;3-9
    • (2002) Mol. Cell Biochem. , vol.234 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 43
    • 0030746621 scopus 로고    scopus 로고
    • The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortial synaptosomal membrane proteins
    • Subramaniam R., Roediger F., Jordan B., Mattson M.P., Keller J.N., Waeg G., Butterfield D.A. The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortial synaptosomal membrane proteins. J. Neurochem. 69:1997;1161-1169
    • (1997) J. Neurochem. , vol.69 , pp. 1161-1169
    • Subramaniam, R.1    Roediger, F.2    Jordan, B.3    Mattson, M.P.4    Keller, J.N.5    Waeg, G.6    Butterfield, D.A.7
  • 44
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. Review: Alzheimer's amyloid β-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
  • 45
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(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
    • 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;25945-25952
    • (1999) J. Biol. Chem. , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 47
    • 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
  • 48
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42)
    • Yatin S.M., Link C.D., Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42). Neurobiol. Aging. 20:1999;325-330
    • (1999) Neurobiol. Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Link, C.D.2    Butterfield, D.A.3
  • 49
    • 0033583252 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-peptide generated free radicals increase rat embryonic neuronal polyamine uptake and ODC activity: Protective effect of Vitamin e
    • Yatin S.M., Yatin M., Aulick T., Ain K.B., Butterfield D.A. Alzheimer's amyloid β-peptide generated free radicals increase rat embryonic neuronal polyamine uptake and ODC activity: protective effect of Vitamin E. Neurosci. Lett. 263:1999;17-20
    • (1999) Neurosci. Lett. , vol.263 , pp. 17-20
    • Yatin, S.M.1    Yatin, M.2    Aulick, T.3    Ain, K.B.4    Butterfield, D.A.5
  • 50
    • 0033788416 scopus 로고    scopus 로고
    • Vitamin e prevents Alzheimer's amyloid β-peptide (1-42)-induced protein oxidation and reactive oxygen species formation
    • Yatin S.M., Varadarajan S., Butterfield D.A. Vitamin E prevents Alzheimer's amyloid β-peptide (1-42)-induced protein oxidation and reactive oxygen species formation. J. Alzheimer's Dis. 2:2000;123-131
    • (2000) J. Alzheimer's Dis. , vol.2 , pp. 123-131
    • Yatin, S.M.1    Varadarajan, S.2    Butterfield, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.