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Volumn 1, Issue 3, 2002, Pages 327-330

Amyloid peptide enhances nail rusting: Novel insight into mechanisms of aging and Alzheimer's disease

Author keywords

Aggregation; Alzheimer's disease; Free radicals; Iron; Neurons; Protein oxidation

Indexed keywords

AMYLOID BETA PROTEIN; CHELATING AGENT; HYDROGEN PEROXIDE; IRON; MEMBRANE LIPID; NUCLEIC ACID; OXYGEN RADICAL; PROTEIN; REACTIVE OXYGEN METABOLITE; SERUM ALBUMIN; WATER; AMYLOID BETA PROTEIN[1-40]; PEPTIDE FRAGMENT;

EID: 0036598956     PISSN: 15681637     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1568-1637(02)00002-8     Document Type: Review
Times cited : (21)

References (12)
  • 2
    • 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.P., 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.P.4    Carney, J.5
  • 4
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82:2002;47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 5
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • Goodman Y., Mattson M.P. Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury. Exp. Neurol. 128:1994;1-12.
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 9
    • 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
  • 10
    • 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;376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 11
    • 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
  • 12
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid β 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.