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Volumn 26, Issue 4, 2005, Pages 665-673

Neurotoxicity and oxidative stress in D1M-substituted Alzheimer's Aβ(1-42): Relevance to N-terminal methionine chemistry in small model peptides

Author keywords

Amyloid beta peptide; Free radicals; Methionine; Neurotoxicity

Indexed keywords

ALPHA TOCOPHEROL; AMINO ACID; AMYLOID BETA PROTEIN[1-42]; ASPARTIC ACID; METHIONINE; NORLEUCINE; REACTIVE OXYGEN METABOLITE; SCAVENGER; SYNTHETIC PEPTIDE;

EID: 14744281174     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2004.11.001     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0033136815 scopus 로고    scopus 로고
    • Vitamin e and other antioxidants in neuroprotection
    • C. Behl Vitamin E and other antioxidants in neuroprotection Int J Vitam Nutr Res 69 1999 213 219
    • (1999) Int J Vitam Nutr Res , vol.69 , pp. 213-219
    • Behl, C.1
  • 2
    • 10844269704 scopus 로고    scopus 로고
    • Role of phenylalanine 20 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • in press.
    • Boyd-Kimball D, Mohmmad Abdul H, Reed T, Sultana R, Butterfield DA, Role of phenylalanine 20 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity. Chem Res Toxicol 2004; in press.
    • (2004) Chem Res Toxicol
    • Boyd-Kimball, D.1    Mohmmad Abdul, H.2    Reed, T.3    Sultana, R.4    Butterfield, D.A.5
  • 3
    • 0036669345 scopus 로고    scopus 로고
    • The radical model of Alzheimer's disease: Specific recognition of Gly29 and Gly33 by Met35 in a beta-sheet model of Abeta: An ONIOM study
    • P. Brunelle, and A. Rauk The radical model of Alzheimer's disease: specific recognition of Gly29 and Gly33 by Met35 in a beta-sheet model of Abeta: an ONIOM study J. Alzheimer's Dis. 4 2002 283 289
    • (2002) J. Alzheimer's Dis. , vol.4 , pp. 283-289
    • Brunelle, P.1    Rauk, A.2
  • 4
    • 0344824654 scopus 로고    scopus 로고
    • Amyloid β-peptide [1-42]-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: Mechanisms and consequences
    • D.A. Butterfield Amyloid β-peptide [1-42]-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences Curr Med Chem 10 2003 2651 2659
    • (2003) Curr Med Chem , vol.10 , pp. 2651-2659
    • Butterfield, D.A.1
  • 5
    • 85030814099 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • in press.
    • Butterfield DA, Boyd-Kimball D, The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim Biophys Acta 2004; in press.
    • (2004) Biochim Biophys Acta
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 6
    • 1842519391 scopus 로고    scopus 로고
    • Alzheimer's amyloid β-peptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide
    • D.A. Butterfield, and A.I. Bush Alzheimer's amyloid β-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide Neurobiol Aging 25 2004 563 568
    • (2004) Neurobiol Aging , vol.25 , pp. 563-568
    • Butterfield, D.A.1    Bush, A.I.2
  • 7
    • 0035997233 scopus 로고    scopus 로고
    • Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid β-peptide 1-42
    • D.A. Butterfield, and J. Kanski 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
  • 8
    • 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
    • D.A. Butterfield, and C.M. Lauderback Lipid peroxidation and protein oxidation in Alzheimer's Disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress Free Rad Biol Med 32 2002 1050 1060
    • (2002) Free Rad Biol Med , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 10
    • 0028706970 scopus 로고
    • Assays of cell viability: Discrimination of cells dying by apoptosis
    • Z. Darzynkiewicz, X. Li, and J. Gong Assays of cell viability: discrimination of cells dying by apoptosis Meth. Cell Biol 41 1994 15 38
    • (1994) Meth. Cell Biol , vol.41 , pp. 15-38
    • Darzynkiewicz, Z.1    Li, X.2    Gong, J.3
  • 13
    • 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
    • J. Kanski, M. Aksenova, and D.A. Butterfield 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
  • 14
    • 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)
    • J. Kanski, M. Aksenova, C. Schöneich, and D.A. Butterfield 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    Schöneich, C.3    Butterfield, D.A.4
  • 15
    • 0037117310 scopus 로고    scopus 로고
    • Role of glycine-33 and methionine-35 in Alzheimer's amyloid β-peptide 1-42-associated oxidative stress and neurotoxicity
    • J. Kanski, S. Varadarajan, M. Aksenova, and D.A. Butterfield Role of glycine-33 and methionine-35 in Alzheimer's amyloid β-peptide 1-42-associated oxidative stress and neurotoxicity Biochim Biophys Acta 1586 2001 190 198
    • (2001) Biochim Biophys Acta , vol.1586 , pp. 190-198
    • Kanski, J.1    Varadarajan, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 16
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • H. LeVine III Quantification of beta-sheet amyloid fibril structures with thioflavin T Meth. Enzymol 309 1999 274 284
    • (1999) Meth. Enzymol , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 17
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • W.R. Markesbery 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
  • 18
    • 0032522103 scopus 로고    scopus 로고
    • One-electron photooxidation of N-methionyl peptides. Mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complexes with oxygen or superoxide
    • B.L. Miller, K. Kuczera, and C. Schoneich One-electron photooxidation of N-methionyl peptides. Mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complexes with oxygen or superoxide J Am Chem Soc 120 1998 3345 3356
    • (1998) J Am Chem Soc , vol.120 , pp. 3345-3356
    • Miller, B.L.1    Kuczera, K.2    Schoneich, C.3
  • 20
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met35 in neurotoxic β-amyloid peptide. A molecular modeling study
    • D. Pogocki, and C. Schöneich Redox properties of Met35 in neurotoxic β-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    Schöneich, C.2
  • 21
    • 1642315515 scopus 로고    scopus 로고
    • Mutation of the Phe20 residue in Alzheimer's amyloid beta-peptide might decrease its toxicity due to disruption of the Met35-cupric site electron transfer pathway
    • D. Pogocki Mutation of the Phe20 residue in Alzheimer's amyloid beta-peptide might decrease its toxicity due to disruption of the Met35-cupric site electron transfer pathway Chem Res Toxicol 17 2004 325 329
    • (2004) Chem Res Toxicol , vol.17 , pp. 325-329
    • Pogocki, D.1
  • 22
    • 0034638379 scopus 로고    scopus 로고
    • Is oxidative damage by β-amyloid and prion peptides mediated by hydrogen atom transfer from glycine α-carbon to methionine sulfur within β-sheets?
    • A. Rauk, D.A. Armstrong, and D.P. Fairlie Is oxidative damage by β-amyloid and prion peptides mediated by hydrogen atom transfer from glycine α-carbon to methionine sulfur within β-sheets? J Am Chem Soc 122 2002 9761 9767
    • (2002) J Am Chem Soc , vol.122 , pp. 9761-9767
    • Rauk, A.1    Armstrong, D.A.2    Fairlie, D.P.3
  • 23
    • 0035081475 scopus 로고    scopus 로고
    • Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • D.J. Selkoe Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein J Alzheimers Dis 3 2001 75 80
    • (2001) J Alzheimers Dis , vol.3 , pp. 75-80
    • Selkoe, D.J.1
  • 24
    • 0025334082 scopus 로고
    • Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro
    • K.V. Subbarao, J.S. Richardson, and L.C. Ang Autopsy samples of Alzheimer's cortex show increased peroxidation in vitro J Neurochem 55 1990 342 345
    • (1990) J Neurochem , vol.55 , pp. 342-345
    • Subbarao, K.V.1    Richardson, J.S.2    Ang, L.C.3
  • 25
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35)
    • S. Varadarajan, J. Kanski, M. Aksenova, C. Lauderback, and D.A. Butterfield 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
  • 26
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity
    • S. Varadarajan, S. Yatin, M. Aksenova, and D.A. Butterfield 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
  • 27
    • 0033133579 scopus 로고    scopus 로고
    • In-vitro and in-vivo oxidative stress associated with Alzheimer's amyloid β-peptide(1-42)
    • S.M. Yatin, S. Varadarajan, C.D. Link, and D.A. Butterfield 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    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 28
    • 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
    • S.M. Yatin, M. Yatin, T. Aulick, K.B. Ain, and D.A. Butterfield 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
  • 29
    • 0033788416 scopus 로고    scopus 로고
    • Vitamin e prevents Alzheimer's amyloid β-peptide (1-42)-induced protein oxidation and reactive oxygen species formation
    • S.M. Yatin, S. Varadarajan, and D.A. Butterfield Vitamin E prevents Alzheimer's amyloid β-peptide (1-42)-induced protein oxidation and reactive oxygen species formation J Alzheimers Dis 2 2000 123 131
    • (2000) J Alzheimers 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.