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Volumn , Issue , 2008, Pages 181-207

Redox Proteomics and Metabolic Proteins in Brain of Subjects with Alzheimer's Disease, Mild Cognitive Impairment, and Models Thereof

Author keywords

Alzheimer's Disease; Energy related proteins; Metabolic proteins; Mild cognitive impairment; Models thereof; Neural degeneration; Neural repair; Oxidative stress; Redox proteomics

Indexed keywords


EID: 84891008660     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527622467.ch9     Document Type: Chapter
Times cited : (2)

References (192)
  • 1
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman, E.R. and Levine, R.L. (2003) Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids, 25 (3-4), 207-218.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 2
    • 0141673128 scopus 로고    scopus 로고
    • Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms
    • Mikkelsen, R.B. and Wardman, P. (2003) Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms. Oncogene, 22 (37), 5734-5754.
    • (2003) Oncogene , vol.22 , Issue.37 , pp. 5734-5754
    • Mikkelsen, R.B.1    Wardman, P.2
  • 3
    • 0033818354 scopus 로고    scopus 로고
    • Ras-dependent and-independent regulation of reactive oxygen species by mitogenic growth factors and TGF-betal
    • Thannickal, V.J., Day, R.M., Klinz, S.G., Bastien, M.C., Larios, J.M. and Fanburg, B.L. (2000) Ras-dependent and-independent regulation of reactive oxygen species by mitogenic growth factors and TGF-betal. FASEB Journal, 14 (12), 1741-1748.
    • (2000) FASEB Journal , vol.14 , Issue.12 , pp. 1741-1748
    • Thannickal, V.J.1    Day, R.M.2    Klinz, S.G.3    Bastien, M.C.4    Larios, J.M.5    Fanburg, B.L.6
  • 6
    • 0034659178 scopus 로고    scopus 로고
    • Glycoxidation and lipoxidation in atherogenesis
    • Baynes, J.W. and Thorpe, S.R. (2000) Glycoxidation and lipoxidation in atherogenesis. Free Radical Biology and Medicine, 28 (12), 1708-1716.
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.12 , pp. 1708-1716
    • Baynes, J.W.1    Thorpe, S.R.2
  • 7
    • 18844440651 scopus 로고    scopus 로고
    • Proteomic identification of proteins oxidized by Abeta(1-42) in synapto-somes: implications for Alzheimer's disease
    • Boyd-Kimball, D., Castegna, A., Sultana, R., Poon, H.F., Petroze, R., Lynn, B.C., Klein, J.B. and Butterfield, D.A. (2005) Proteomic identification of proteins oxidized by Abeta(1-42) in synapto-somes: implications for Alzheimer's disease. Brain Research, 1044 (2), 206-215.
    • (2005) Brain Research , vol.1044 , Issue.2 , pp. 206-215
    • Boyd-Kimball, D.1    Castegna, A.2    Sultana, R.3    Poon, H.F.4    Petroze, R.5    Lynn, B.C.6    Klein, J.B.7    Butterfield, D.A.8
  • 8
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield, D.A. (2002) Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radical Research, 36 (12), 1307-1313.
    • (2002) Free Radical Research , vol.36 , Issue.12 , pp. 1307-1313
    • Butterfield, D.A.1
  • 9
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics
    • Butterfield, D.A., Perluigi, M. and Sultana, R. (2006) Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. European Journal of Pharmacology, 545 (1), 39-50.
    • (2006) European Journal of Pharmacology , vol.545 , Issue.1 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 10
    • 0027522231 scopus 로고
    • Redox regulation of a src family protein tyrosine kinase p56lck in T cells
    • Nakamura, K., Hori, T., Sato, N., Sugie, K., Kawakami, T. and Yodoi, J. (1993) Redox regulation of a src family protein tyrosine kinase p56lck in T cells. Oncogene, 8 (11), 3133-3139.
    • (1993) Oncogene , vol.8 , Issue.11 , pp. 3133-3139
    • Nakamura, K.1    Hori, T.2    Sato, N.3    Sugie, K.4    Kawakami, T.5    Yodoi, J.6
  • 11
    • 0029677843 scopus 로고    scopus 로고
    • Alzheimer disease: protein-protein interaction and oxidative stress
    • Smith, M.A. and Perry, G. (1996) Alzheimer disease: protein-protein interaction and oxidative stress. Boletin de Estudios Medicos Y Biologicos, 44 (1-4), 5-10.
    • (1996) Boletin de Estudios Medicos Y Biologicos , vol.44 , Issue.1-4 , pp. 5-10
    • Smith, M.A.1    Perry, G.2
  • 15
    • 0035072229 scopus 로고    scopus 로고
    • Degradationof oxidized proteins by the 20S proteasome
    • Davies, K.J. (2001) Degradationof oxidized proteins by the 20S proteasome. Biochimie, 83 (3-4), 301-310.
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 301-310
    • Davies, K.J.1
  • 16
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. (2000) Quantification and significance of protein oxidation in biological samples. Drug Metabolism Reviews, 32 (3-4), 307-326.
    • (2000) Drug Metabolism Reviews , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 17
    • 0027380609 scopus 로고
    • Nitric oxide superoxide and peroxynitrite: putative mediators of NMDA-induced cell death in cerebellar granule cells
    • Lafon-Cazal, M., Culcasi, M., Gaven, F., Pietri, S. and Bockaert, J. (1993) Nitric oxide superoxide and peroxynitrite: putative mediators of NMDA-induced cell death in cerebellar granule cells. Neuropharmacology, 32 (11), 1259-1266.
    • (1993) Neuropharmacology , vol.32 , Issue.11 , pp. 1259-1266
    • Lafon-Cazal, M.1    Culcasi, M.2    Gaven, F.3    Pietri, S.4    Bockaert, J.5
  • 18
    • 0347991813 scopus 로고    scopus 로고
    • Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: a nutritional approach
    • Calabrese, V., Scapagnini, G., Colombrita, C., Ravagna, A., Pennisi, G., Giuffrida Stella, A.M., Galli, F. and Butterfield, D.A. (2003) Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: a nutritional approach. Amino Acids, 25 (3-4), 437-444.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 437-444
    • Calabrese, V.1    Scapagnini, G.2    Colombrita, C.3    Ravagna, A.4    Pennisi, G.5    Giuffrida Stella, A.M.6    Galli, F.7    Butterfield, D.A.8
  • 19
    • 0041378078 scopus 로고    scopus 로고
    • Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine
    • Calabrese, V., Scapagnini, G., Ravagna, A., Bella, R., Butterfield, D.A., Calvani, M., Pennisi, G. and Giuffrida Stella, A.M. (2003) Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochemical Research, 28 (9), 1321-1328.
    • (2003) Neurochemical Research , vol.28 , Issue.9 , pp. 1321-1328
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Bella, R.4    Butterfield, D.A.5    Calvani, M.6    Pennisi, G.7    Giuffrida Stella, A.M.8
  • 21
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E.R. and Berlett, B.S. (1997) Reactive oxygen-mediated protein oxidation in aging and disease. Chemical Research in Toxicology, 10 (5), 485-494.
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 22
    • 2142815107 scopus 로고    scopus 로고
    • Regeneration ofperoxiredoxins by p53-regulated sestrins homologs of bacterial AhpD
    • Budanov, A.V., Sablina, A.A., Feinstein, E., Koonin, E.V. and Chumakov, P.M. (2004) Regeneration ofperoxiredoxins by p53-regulated sestrins homologs of bacterial AhpD. Science, 304 (5670), 596-600.
    • (2004) Science , vol.304 , Issue.5670 , pp. 596-600
    • Budanov, A.V.1    Sablina, A.A.2    Feinstein, E.3    Koonin, E.V.4    Chumakov, P.M.5
  • 24
    • 84889411742 scopus 로고    scopus 로고
    • Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases
    • John Wiley & Sons, Ltd, Hoboken, NJ.
    • Dalle-Donne, I., Scaloni, A. and Butterfield, D.A. (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases, John Wiley & Sons, Ltd, Hoboken, NJ.
    • (2006)
    • Dalle-Donne, I.1    Scaloni, A.2    Butterfield, D.A.3
  • 26
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune, T., Reinheckel, T. and Davies, K.J. (1997) Degradation of oxidized proteins in mammalian cells. FASEB Journal, 11 (7), 526-534.
    • (1997) FASEB Journal , vol.11 , Issue.7 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 27
    • 0024253948 scopus 로고
    • Implication of protein oxidation in protein turnover aging, and oxygen toxicity
    • Stadtman, E.R., Oliver, C.N., Levine, R.L., Fucci, L. and Rivett, A.J. (1988) Implication of protein oxidation in protein turnover aging, and oxygen toxicity. Basic Life Science, 49, 331-339.
    • (1988) Basic Life Science , vol.49 , pp. 331-339
    • Stadtman, E.R.1    Oliver, C.N.2    Levine, R.L.3    Fucci, L.4    Rivett, A.J.5
  • 29
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: examination by Western blot immunoassay
    • Shacter, E., Williams, J.A., Lim, M. and Levine, R.L. (1994) Differential susceptibility of plasma proteins to oxidative modification: examination by Western blot immunoassay. Free Radical Biology and Medicine, 17 (5), 429-437.
    • (1994) Free Radical Biology and Medicine , vol.17 , Issue.5 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 30
  • 32
    • 0024788456 scopus 로고
    • Protein oxidation and proteolysis during aging and oxidative stress
    • Starke-Reed, P.E. and Oliver, C.N. (1989) Protein oxidation and proteolysis during aging and oxidative stress. Archives of Biochemistry and Biophysics, 275 (2), 559-567.
    • (1989) Archives of Biochemistry and Biophysics , vol.275 , Issue.2 , pp. 559-567
    • Starke-Reed, P.E.1    Oliver, C.N.2
  • 34
    • 0023020327 scopus 로고
    • Regulation of intracellular protein turnover: covalent modification as a mechanism ofmarking proteins for degradation
    • Rivett, A.J. (1986) Regulation of intracellular protein turnover: covalent modification as a mechanism ofmarking proteins for degradation. Current Topics in Cellular Regulation, 28, 291-337.
    • (1986) Current Topics in Cellular Regulation , vol.28 , pp. 291-337
    • Rivett, A.J.1
  • 35
  • 37
    • 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: the role of Abeta 1-42
    • Lauderback, C.M., Hackett, J.M., Huang, F.F., Keller, J.N., Szweda, L.I., Markesbery, W.R. and Butterfield, D.A. (2001) The glial glutamate transporter GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Abeta 1-42. Journal of Neurochemistry, 78 (2), 413-416.
    • (2001) Journal of Neurochemistry , vol.78 , Issue.2 , 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    Butterfield, D.A.7
  • 38
    • 11144261790 scopus 로고    scopus 로고
    • Oxidatively modified GSTand MRP1 in Alzheimer's disease brain: implications for accumulation of reactive lipid peroxidation products
    • Sultana, R. and Butterfield, D.A. (2004) Oxidatively modified GSTand MRP1 in Alzheimer's disease brain: implications for accumulation of reactive lipid peroxidation products. Neurochemical Research, 29, 2215-2220.
    • (2004) Neurochemical Research , vol.29 , pp. 2215-2220
    • Sultana, R.1    Butterfield, D.A.2
  • 39
    • 0036123645 scopus 로고    scopus 로고
    • Increased protein oxidation and decreased creatine kinase BB expression and activity after spinal cord contusion injury
    • Aksenova, M., Butterfield, D.A., Zhang, S.X., Underwood, M. and Geddes, J.W. (2002) Increased protein oxidation and decreased creatine kinase BB expression and activity after spinal cord contusion injury. Journal of Neurotrauma, 19 (4), 491-502.
    • (2002) Journal of Neurotrauma , vol.19 , Issue.4 , pp. 491-502
    • Aksenova, M.1    Butterfield, D.A.2    Zhang, S.X.3    Underwood, M.4    Geddes, J.W.5
  • 40
    • 0036375410 scopus 로고    scopus 로고
    • Genomes proteomes, and dynamic networks in the cell nucleus
    • Roix, J. and Misteli, T. (2002) Genomes proteomes, and dynamic networks in the cell nucleus. Histochemistry and Cell Biology, 118 (2), 105-116.
    • (2002) Histochemistry and Cell Biology , vol.118 , Issue.2 , pp. 105-116
    • Roix, J.1    Misteli, T.2
  • 41
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains
    • Rabilloud, T. (2002) Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics, 2, 3-10.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 42
    • 0036424759 scopus 로고    scopus 로고
    • Investigation of cytolysin variants by peptide mapping: enhanced protein characterization using complementary ionization and mass spectrometric techniques
    • Stevens, S.M., Jr, Kem, W.R. and Prokai, L. (2002) Investigation of cytolysin variants by peptide mapping: enhanced protein characterization using complementary ionization and mass spectrometric techniques. Rapid Communications in Mass Spectrometry, 16 (22), 2094-2101.
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.22 , pp. 2094-2101
    • Stevens Jr., S.M.1    Kem, W.R.2    Prokai, L.3
  • 44
    • 0035477025 scopus 로고    scopus 로고
    • Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis
    • Smolka, M.B., Zhou, H., Purkayastha, S. and Aebersold, R. (2001) Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis. Analytical Biochemistry, 297 (1), 25-31.
    • (2001) Analytical Biochemistry , vol.297 , Issue.1 , pp. 25-31
    • Smolka, M.B.1    Zhou, H.2    Purkayastha, S.3    Aebersold, R.4
  • 46
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. The Journal of Biological Chemistry, 250 (10), 4007-4021.
    • (1975) The Journal of Biological Chemistry , vol.250 , Issue.10 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 48
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni, V., Molloy, M. and Rabilloud, T. (2000) Membrane proteins and proteomics: un amour impossible? Electrophoresis, 21 (6), 1054-1070.
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 49
    • 33745990556 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease
    • Boyd-Kimball, D., Poon, H.F., Lynn, B.C., Cai, J., Pierce, W.M., Jr, Klein, J.B., Ferguson, J., Link, C.D. and Butterfield, D.A. (2006) Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease. Neurobiology of Aging, 27 (9), 1239-1249.
    • (2006) Neurobiology of Aging , vol.27 , Issue.9 , pp. 1239-1249
    • Boyd-Kimball, D.1    Poon, H.F.2    Lynn, B.C.3    Cai, J.4    Pierce Jr., W.M.5    Klein, J.B.6    Ferguson, J.7    Link, C.D.8    Butterfield, D.A.9
  • 51
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal, M.F. (1998) Mitochondrial dysfunction in neurodegenerative diseases. Biochimica et Biophysica Acta, 1366 (1-2), 211-223.
    • (1998) Biochimica et Biophysica Acta , vol.1366 , Issue.1-2 , pp. 211-223
    • Beal, M.F.1
  • 53
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimers disease brain and in vivo and in vitro models of AD centered around Abeta (1-42)
    • Sultana, R., Perluigi, M. and Butterfield, D.A. (2006) Redox proteomics identification of oxidatively modified proteins in Alzheimers disease brain and in vivo and in vitro models of AD centered around Abeta (1-42). Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 833 (1), 3-11.
    • (2006) Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences , vol.833 , Issue.1 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 54
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman, R. and Saitoh, T. (1991) Advances in Alzheimer's disease. FASEB Journal, 5 (3), 278-286.
    • (1991) FASEB Journal , vol.5 , Issue.3 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 58
    • 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. and Castegna, A. (2001) Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends in Molecular Medicine, 7 (12), 548-554.
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.12 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 60
    • 3042693940 scopus 로고    scopus 로고
    • Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer's disease
    • Hynd, M.R., Scott, H.L. and Dodd, P.R. (2004) Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer's disease. Neurochemistry International, 45 (5), 583-595.
    • (2004) Neurochemistry International , vol.45 , Issue.5 , pp. 583-595
    • Hynd, M.R.1    Scott, H.L.2    Dodd, P.R.3
  • 61
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W.R. (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radical Biology and Medicine, 23 (1), 134-147.
    • (1997) Free Radical Biology and Medicine , vol.23 , Issue.1 , pp. 134-147
    • Markesbery, W.R.1
  • 62
    • 0141705360 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: implications for the pathogenesis of neurodegenerative diseases
    • Rego, A.C. and Oliveira, C.R. (2003) Mitochondrial dysfunction and reactive oxygen species in excitotoxicity and apoptosis: implications for the pathogenesis of neurodegenerative diseases. Neurochemical Research, 28 (10), 1563-1574.
    • (2003) Neurochemical Research , vol.28 , Issue.10 , pp. 1563-1574
    • Rego, A.C.1    Oliveira, C.R.2
  • 64
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: cause effect, or association?
    • Ischiropoulos, H. and Beckman, J.S. (2003) Oxidative stress and nitration in neurodegeneration: cause effect, or association? Journal of Clinical Investigation, 111 (2), 163-169.
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.2 , pp. 163-169
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 65
    • 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
    • Butterfield, D.A. and Lauderback, C.M. (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress. Free Radical Biology and Medicine, 32 (11), 1050-1060.
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 66
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery, W.R. and Carney, J.M. (1999) Oxidative alterations in Alzheimer's disease. Brain Pathology, 9 (1), 133-146.
    • (1999) Brain Pathology , vol.9 , Issue.1 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 67
    • 0033751421 scopus 로고    scopus 로고
    • Metabolic metallic, and mitotic sources of oxidative stress in Alzheimer disease
    • Smith, M.A., Nunomura, A., Zhu, X., Takeda, A. and Perry, G. (2000) Metabolic metallic, and mitotic sources of oxidative stress in Alzheimer disease. Antioxidants and Redox Signalling, 2 (3), 413-420.
    • (2000) Antioxidants and Redox Signalling , vol.2 , Issue.3 , pp. 413-420
    • Smith, M.A.1    Nunomura, A.2    Zhu, X.3    Takeda, A.4    Perry, G.5
  • 69
    • 14144255339 scopus 로고    scopus 로고
    • Nutritional antioxidants and the heme oxygenase pathway of stress tolerance: novel targets for neuropro-tection in Alzheimer's disease
    • Calabrese, V., Butterfield, D.A. and Stella, A.M. (2003) Nutritional antioxidants and the heme oxygenase pathway of stress tolerance: novel targets for neuropro-tection in Alzheimer's disease. Italian Journal of Biochemistry, 52 (4), 177-181.
    • (2003) Italian Journal of Biochemistry , vol.52 , Issue.4 , pp. 177-181
    • Calabrese, V.1    Butterfield, D.A.2    Stella, A.M.3
  • 70
    • 15744398884 scopus 로고    scopus 로고
    • Oxidative modifications and aggregation of Cu Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases
    • Choi, J., Rees, H.D., Weintraub, S.T., Levey, A.I., Chin, L.S. and Li, L. (2005) Oxidative modifications and aggregation of Cu Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases. The Journal of Biological Chemistry, 280 (12), 11648-11655.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11648-11655
    • Choi, J.1    Rees, H.D.2    Weintraub, S.T.3    Levey, A.I.4    Chin, L.S.5    Li, L.6
  • 71
    • 0037096194 scopus 로고    scopus 로고
    • Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease
    • Dore, S. (2002) Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease. Free Radical Biology and Medicine, 32 (12), 1276-1282.
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1276-1282
    • Dore, S.1
  • 72
    • 0029073455 scopus 로고
    • Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease
    • Lovell, M.A., Ehmann, W.D., Butler, S.M. and Markesbery, W.R. (1995) Elevated thiobarbituric acid-reactive substances and antioxidant enzyme activity in the brain in Alzheimer's disease. Neurology, 45 (8), 1594-1601.
    • (1995) Neurology , vol.45 , Issue.8 , pp. 1594-1601
    • Lovell, M.A.1    Ehmann, W.D.2    Butler, S.M.3    Markesbery, W.R.4
  • 73
    • 0033969616 scopus 로고    scopus 로고
    • Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain
    • Lovell, M.A., Xie, C., Gabbita, S.P. and Markesbery, W.R. (2000) Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain. Free Radical Biology and Medicine, 28 (3), 418-427.
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.3 , pp. 418-427
    • Lovell, M.A.1    Xie, C.2    Gabbita, S.P.3    Markesbery, W.R.4
  • 77
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • Sayre, L.M., Zelasko, D.A., Harris, P.L., Perry, G., Salomon, R.G. and Smith, M.A. (1997) 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. Journal of Neurochemistry, 68 (5), 2092-2097.
    • (1997) Journal of Neurochemistry , vol.68 , Issue.5 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3    Perry, G.4    Salomon, R.G.5    Smith, M.A.6
  • 79
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Pratico, D., Uryu, K., Leight, S., Trojanoswki, J.Q. and Lee, V.M. (2001) Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. Journal of Neuroscience, 21 (12), 4183-4187.
    • (2001) Journal of Neuroscience , vol.21 , Issue.12 , pp. 4183-4187
    • Pratico, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 80
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • Yan, S.D., Yan, S.F., Chen, X., Fu, J., Chen, M., Kuppusamy, P., Smith, M.A., Perry, G., Godman, G.C., Nawroth, P., Zweier, J.L. and Stern, D. (1995) Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nature Medicine, 1 (7), 693-699.
    • (1995) Nature Medicine , vol.1 , Issue.7 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10    Zweier, J.L.11    Stern, D.12
  • 81
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model
    • Drake, J., Link, C.D. and Butterfield, D.A. (2003) Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model. Neurobiology of Aging, 24 (3), 415-420.
    • (2003) Neurobiology of Aging , vol.24 , Issue.3 , pp. 415-420
    • Drake, J.1    Link, C.D.2    Butterfield, D.A.3
  • 82
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta 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., Beyreuther, K., Barrow, C.J., Masters, C.L., Bush, A.I. and Barnham, K.J. (2001) Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. Journal of Biological Chemistry, 276 (23), 20466-20473.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.23 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 84
    • 0037174856 scopus 로고    scopus 로고
    • Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine cholesterol, and biological reducing agents to neurotoxic H(2)O(2)
    • Opazo, C., Huang, X., Cherny, R.A., Moir, R.D., Roher, A.E., White, A.R., Cappai, R., Masters, C.L., Tanzi, R.E., Inestrosa, N.C. and Bush, A.I. (2002) Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine cholesterol, and biological reducing agents to neurotoxic H(2)O(2). The Journal of Biological Chemistry, 277 (43), 40302-40308.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40302-40308
    • Opazo, C.1    Huang, X.2    Cherny, R.A.3    Moir, R.D.4    Roher, A.E.5    White, A.R.6    Cappai, R.7    Masters, C.L.8    Tanzi, R.E.9    Inestrosa, N.C.10    Bush, A.I.11
  • 85
    • 0037096251 scopus 로고    scopus 로고
    • A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage
    • Zou, K., Gong, J.S., Yanagisawa, K. and Michikawa, M. (2002) A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. Journal of Neuroscience, 22 (12), 4833-4841.
    • (2002) Journal of Neuroscience , vol.22 , Issue.12 , pp. 4833-4841
    • Zou, K.1    Gong, J.S.2    Yanagisawa, K.3    Michikawa, M.4
  • 86
    • 1842528400 scopus 로고    scopus 로고
    • Convergence of atherosclerosis and Alzheimer's disease: inflammation cholesterol, and misfolded proteins
    • Casserly, I. and Topol, E. (2004) Convergence of atherosclerosis and Alzheimer's disease: inflammation cholesterol, and misfolded proteins. Lancet, 363 (9415), 1139-1146.
    • (2004) Lancet , vol.363 , Issue.9415 , pp. 1139-1146
    • Casserly, I.1    Topol, E.2
  • 87
    • 0028293628 scopus 로고
    • Microglial oxyradical production: causes and consequences
    • Colton, C.A. (1994) Microglial oxyradical production: causes and consequences. Neuropathology and Applied Neurobiology, 20 (2), 208-209.
    • (1994) Neuropathology and Applied Neurobiology , vol.20 , Issue.2 , pp. 208-209
    • Colton, C.A.1
  • 88
    • 33645106304 scopus 로고    scopus 로고
    • Mutations in amyloid precursor protein and presenilin-1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid beta-peptide (1-42) HO and kainic acid: implications for Alzheimer's disease
    • Mohmmad Abdul, H., Sultana, R., Keller, J.N., St Clair, D.K., Markesbery, W.R. and Butterfield, D.A. (2006) Mutations in amyloid precursor protein and presenilin-1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid beta-peptide (1-42) HO and kainic acid: implications for Alzheimer's disease. Journal of Neurochemistry, 96 (5), 1322-1335.
    • (2006) Journal of Neurochemistry , vol.96 , Issue.5 , pp. 1322-1335
    • Mohmmad Abdul, H.1    Sultana, R.2    Keller, J.N.3    St Clair, D.K.4    Markesbery, W.R.5    Butterfield, D.A.6
  • 89
    • 12844257538 scopus 로고    scopus 로고
    • Alzheimer's disease, oxidative injury, and cytokines
    • discussion
    • Summers, W.K. (2004) Alzheimer's disease, oxidative injury, and cytokines. Journal of Alzheimer's Disease, 6 (6), 651-657, discussion 673-681.
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.6
    • Summers, W.K.1
  • 90
    • 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., Booze, R., Markesbery, W.R. and Butterfield, D.A. (2002) 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 Radical Biology and Medicine, 33 (4), 562-571.
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.4 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 91
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2 alpha-enolase and heat shock cognate 71
    • Castegna, A., Aksenov, M., Thongboonkerd, V., Klein, J.B., Pierce, W.M., Booze, R., Markesbery, W.R. and Butterfield, D.A. (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2 alpha-enolase and heat shock cognate 71. Journal of Neurochemistry, 82 (6), 1524-1532.
    • (2002) Journal of Neurochemistry , vol.82 , Issue.6 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 93
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD
    • Sultana, R., Boyd-Kimball, D., Poon, H.F., Cai, J., Pierce, W.M., Klein, J.B., Merchant, M., Markesbery, W.R. and Butterfield, D.A. (2006) Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neuro-biology of Aging, 27 (11), 1564-1576.
    • (2006) Neuro-biology of Aging , vol.27 , Issue.11 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 95
    • 0242440004 scopus 로고    scopus 로고
    • Aberrant profiles of native and oxidized glycoproteins in Alzheimer plasma
    • Yu, H.L., Chertkow, H.M., Bergman, H. and Schipper, H.M. (2003) Aberrant profiles of native and oxidized glycoproteins in Alzheimer plasma. Proteomics, 3 (11), 2240-2248.
    • (2003) Proteomics , vol.3 , Issue.11 , pp. 2240-2248
    • Yu, H.L.1    Chertkow, H.M.2    Bergman, H.3    Schipper, H.M.4
  • 97
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley, K., Maidt, M.L., Yu, Z., Sang, H., Markesbery, W.R. and Floyd, R.A. (1998) Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. Journal of Neuroscience, 18 (20), 8126-8132.
    • (1998) Journal of Neuroscience , vol.18 , Issue.20 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 98
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease
    • Butterfield, D.A., Poon, H.F., St Clair, D., Keller, J.N., Pierce, W.M., Klein, J.B. and " Markesbery, W.R. (2006) Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiology of Disease, 22 (2), 223-232.
    • (2006) Neurobiology of Disease , vol.22 , Issue.2 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 99
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi, J., Levey, A.I., Weintraub, S.T., Rees, H.D., Gearing, M., Chin, L.S. and Li, L. (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. Journal of Biological Chemistry, 279 (13), 13256-13264.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 100
    • 33747199933 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory
    • Gong, B., Cao, Z., Zheng, P., Vitolo, O.V., Liu, S., Staniszewski, A., Moolman, D., Zhang, H., Shelanski, M. and Arancio, O. (2006) Ubiquitin hydrolase Uch-L1 rescues beta-amyloid-induced decreases in synaptic function and contextual memory. Cell, 126 (4), 775-788.
    • (2006) Cell , vol.126 , Issue.4 , pp. 775-788
    • Gong, B.1    Cao, Z.2    Zheng, P.3    Vitolo, O.V.4    Liu, S.5    Staniszewski, A.6    Moolman, D.7    Zhang, H.8    Shelanski, M.9    Arancio, O.10
  • 101
    • 0023792365 scopus 로고
    • Energy metabolism in disorders of the nervous system
    • Blass, J.P., Sheu, R.K. and Cedarbaum, J.M. (1988) Energy metabolism in disorders of the nervous system. Revue Neurologique (Paris), 144 (10), 543-563.
    • (1988) Revue Neurologique (Paris) , vol.144 , Issue.10 , pp. 543-563
    • Blass, J.P.1    Sheu, R.K.2    Cedarbaum, J.M.3
  • 102
    • 0034103586 scopus 로고    scopus 로고
    • Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise
    • Blass, J.P., Sheu, R.K. and Gibson, G.E. (2000) Inherent abnormalities in energy metabolism in Alzheimer disease. Interaction with cerebrovascular compromise. Annals of the New York Academy of Sciences, 903, 204-221.
    • (2000) Annals of the New York Academy of Sciences , vol.903 , pp. 204-221
    • Blass, J.P.1    Sheu, R.K.2    Gibson, G.E.3
  • 103
    • 0034007860 scopus 로고    scopus 로고
    • Glucose metabolism in the developing brain
    • Vannucci, R.C. and Vannucci, S.J. (2000) Glucose metabolism in the developing brain. Seminars in Perinatology, 24 (2), 107-115.
    • (2000) Seminars in Perinatology , vol.24 , Issue.2 , pp. 107-115
    • Vannucci, R.C.1    Vannucci, S.J.2
  • 104
    • 0028872813 scopus 로고
    • Functional alterations in Alzheimer's disease: decreased glucose transporter 3 immunoreactivity in the perforant pathway terminal zone
    • Harr, S.D., Simonian, N.A. and Hyman, B.T. (1995) Functional alterations in Alzheimer's disease: decreased glucose transporter 3 immunoreactivity in the perforant pathway terminal zone. Journal of Neuropathology and Experimental Neurology, 54 (1), 38-41.
    • (1995) Journal of Neuropathology and Experimental Neurology , vol.54 , Issue.1 , pp. 38-41
    • Harr, S.D.1    Simonian, N.A.2    Hyman, B.T.3
  • 105
    • 0029869755 scopus 로고    scopus 로고
    • Glucose regulation and cognitive functions: relation to Alzheimer's disease and diabetes
    • Messier, C. and Gagnon, M. (1996) Glucose regulation and cognitive functions: relation to Alzheimer's disease and diabetes. Behavioural Brain Research, 75 (1-2), 1-11.
    • (1996) Behavioural Brain Research , vol.75 , Issue.1-2 , pp. 1-11
    • Messier, C.1    Gagnon, M.2
  • 106
    • 0342980328 scopus 로고    scopus 로고
    • in vivo PETimaging and postmortem studies suggest potentially reversible and irreversible stages of brain metabolic failure in Alzheimer's disease
    • Rapoport, S.I. (1999) in vivo PETimaging and postmortem studies suggest potentially reversible and irreversible stages of brain metabolic failure in Alzheimer's disease. European Archives of Psychiatry and Clinical Neuroscience, 249 (Suppl. 3), 46-55.
    • (1999) European Archives of Psychiatry and Clinical Neuroscience , vol.249 , Issue.SUPPL. 3 , pp. 46-55
    • Rapoport, S.I.1
  • 107
    • 0031797832 scopus 로고    scopus 로고
    • Glucose intolerance cognitive impairment and Alzheimer's disease
    • Vanhanen, M. and Soininen, H. (1998) Glucose intolerance cognitive impairment and Alzheimer's disease. Current Opinion in Neurology, 11 (6), 673-677.
    • (1998) Current Opinion in Neurology , vol.11 , Issue.6 , pp. 673-677
    • Vanhanen, M.1    Soininen, H.2
  • 108
    • 0029814577 scopus 로고    scopus 로고
    • Hippocampal damage and cytoskeletal disruption resulting from impaired energy metabolism. Implications for Alzheimer disease
    • Geddes, J.W., Pang, Z. and Wiley, D.H. (1996) Hippocampal damage and cytoskeletal disruption resulting from impaired energy metabolism. Implications for Alzheimer disease. Molecular and Chemical Neuropathology, 28 (1-3), 65-74.
    • (1996) Molecular and Chemical Neuropathology , vol.28 , Issue.1-3 , pp. 65-74
    • Geddes, J.W.1    Pang, Z.2    Wiley, D.H.3
  • 111
    • 0026659777 scopus 로고
    • Glucose deprivation elicits neuro-fibrillary tangle-like antigenic changes in hippocampal neurons: prevention by NGF and bFGF
    • Cheng, B. and Mattson, M.P. (1992) Glucose deprivation elicits neuro-fibrillary tangle-like antigenic changes in hippocampal neurons: prevention by NGF and bFGF. Experimental Neurology, 117 (2), 114-123.
    • (1992) Experimental Neurology , vol.117 , Issue.2 , pp. 114-123
    • Cheng, B.1    Mattson, M.P.2
  • 112
    • 1642341492 scopus 로고    scopus 로고
    • Modulation of phospho-lipid asymmetry in synaptosomal membranes by the lipid peroxidation products 4-hydroxynonenal and acrolein: implications for Alzheimer's disease
    • Castegna, A., Lauderback, C.M., Mohmmad-Abdul, H. and Butterfield, D.A. (2004) Modulation of phospho-lipid asymmetry in synaptosomal membranes by the lipid peroxidation products 4-hydroxynonenal and acrolein: implications for Alzheimer's disease. Brain Research, 1004 (1-2), 193-197.
    • (2004) Brain Research , vol.1004 , Issue.1-2 , pp. 193-197
    • Castegna, A.1    Lauderback, C.M.2    Mohmmad-Abdul, H.3    Butterfield, D.A.4
  • 113
    • 20444451750 scopus 로고    scopus 로고
    • Protection against amyloid beta-peptide (1-42)-induced loss of phospholipid asymmetry in synapto-somal membranes by tricyclodecan-9-xanthogenate (D609) and ferulic acid ethyl ester: implications for Alzheimer's disease
    • Mohmmad Abdul, H. and Butterfield, D.A. (2005) Protection against amyloid beta-peptide (1-42)-induced loss of phospholipid asymmetry in synapto-somal membranes by tricyclodecan-9-xanthogenate (D609) and ferulic acid ethyl ester: implications for Alzheimer's disease. Biochimica et Biophysica Acta, 1741 (1-2), 140-148.
    • (2005) Biochimica et Biophysica Acta , vol.1741 , Issue.1-2 , pp. 140-148
    • Mohmmad Abdul, H.1    Butterfield, D.A.2
  • 114
    • 12144289492 scopus 로고    scopus 로고
    • Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: implications for Alzheimer's disease
    • Planel, E., Miyasaka, T., Launey, T., Chui, D.H., Tanemura, K., Sato, S., Murayama, O., Ishiguro, K., Tatebayashi, Y. and Takashima, A. (2004) Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: implications for Alzheimer's disease. Journal of Neuroscience, 24 (10), 2401-2411.
    • (2004) Journal of Neuroscience , vol.24 , Issue.10 , pp. 2401-2411
    • Planel, E.1    Miyasaka, T.2    Launey, T.3    Chui, D.H.4    Tanemura, K.5    Sato, S.6    Murayama, O.7    Ishiguro, K.8    Tatebayashi, Y.9    Takashima, A.10
  • 115
    • 0019142890 scopus 로고
    • Glycolytic enzymes from human autoptic brain cortex: normal aged and demented cases
    • Iwangoff, P., Armbruster, R., Enz, A. and Meier-Ruge, W. (1980) Glycolytic enzymes from human autoptic brain cortex: normal aged and demented cases. Mechanisms of Ageingand Development, 14 (1-2), 203-209.
    • (1980) Mechanisms of Ageingand Development , vol.14 , Issue.1-2 , pp. 203-209
    • Iwangoff, P.1    Armbruster, R.2    Enz, A.3    Meier-Ruge, W.4
  • 117
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: an electrochemical transducer with rotatory mechanics
    • Junge, W., Lill, H. and Engelbrecht, S. (1997) ATP synthase: an electrochemical transducer with rotatory mechanics. Trends in Biochemical Sciences, 22 (11), 420-423.
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.11 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 119
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H. and Yankner, B.A. (2002) Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron, 33 (5), 677-688.
    • (2002) Neuron , vol.33 , Issue.5 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6    Yankner, B.A.7
  • 120
    • 4544335597 scopus 로고    scopus 로고
    • Mild cognitive impairment as a diagnostic entity
    • Petersen, R.C. (2004) Mild cognitive impairment as a diagnostic entity. Journal of Internal Medicine, 256 (3), 183-194.
    • (2004) Journal of Internal Medicine , vol.256 , Issue.3 , pp. 183-194
    • Petersen, R.C.1
  • 123
    • 4444364872 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor apolipoprotein E genetic variants and cognitive performance in Alzheimer's disease
    • Nacmias, B., Piccini, C., Bagnoli, S., Tedde, A., Cellini, E., Bracco, L. and Sorbi, S. (2004) Brain-derived neurotrophic factor apolipoprotein E genetic variants and cognitive performance in Alzheimer's disease. Neuroscience Letters, 367 (3), 379-383.
    • (2004) Neuroscience Letters , vol.367 , Issue.3 , pp. 379-383
    • Nacmias, B.1    Piccini, C.2    Bagnoli, S.3    Tedde, A.4    Cellini, E.5    Bracco, L.6    Sorbi, S.7
  • 124
    • 0037111448 scopus 로고    scopus 로고
    • Apolipoprotein E epsilon 4 allele frequency in demented and cognitively impaired patients with and without cerebrovascular disease
    • Traykov, L., Rigaud, A.S., Baudic, S., Smagghe, A., Boller, F. and Forette, F. (2002) Apolipoprotein E epsilon 4 allele frequency in demented and cognitively impaired patients with and without cerebrovascular disease. Journal of the Neurological Sciences, 203-204, 177-181.
    • (2002) Journal of the Neurological Sciences , vol.203-204 , pp. 177-181
    • Traykov, L.1    Rigaud, A.S.2    Baudic, S.3    Smagghe, A.4    Boller, F.5    Forette, F.6
  • 125
    • 24044472067 scopus 로고    scopus 로고
    • Vitamin E and donepezil for the treatment ofmild cognitive impairment
    • author reply
    • Barnes, D.E. and Yaffe, K. (2005) Vitamin E and donepezil for the treatment ofmild cognitive impairment. New England Journal of Medicine, 353 (9), 951-952, author reply 951-952.
    • (2005) New England Journal of Medicine , vol.353 , Issue.9
    • Barnes, D.E.1    Yaffe, K.2
  • 129
    • 33644987632 scopus 로고    scopus 로고
    • Elevated protein-bound levels of the lipid peroxidation product 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment
    • Butterfield, D.A., Reed, T., Perluigi, M., De Marco, C., Coccia, R., Cini, C. and Sultana, R. (2006) Elevated protein-bound levels of the lipid peroxidation product 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment. Neuroscience Letters, 397 (3), 170-173.
    • (2006) Neuroscience Letters , vol.397 , Issue.3 , pp. 170-173
    • Butterfield, D.A.1    Reed, T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Cini, C.6    Sultana, R.7
  • 131
    • 33745096512 scopus 로고    scopus 로고
    • Decreased RNA and increased RNA oxidation, in Ribosomes from early Alzheimer's disease
    • Ding, Q., Markesbery, W.R., Cecarini, V. and Keller, J.N. (2006) Decreased RNA and increased RNA oxidation, in Ribosomes from early Alzheimer's disease. Neurochemical Research. 31 (5), 705-710.
    • (2006) Neurochemical Research , vol.31 , Issue.5 , pp. 705-710
    • Ding, Q.1    Markesbery, W.R.2    Cecarini, V.3    Keller, J.N.4
  • 132
    • 33645106680 scopus 로고    scopus 로고
    • Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment
    • Wang, J., Markesbery, W.R. and Lovell, M.A. (2006) Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment. Journal of Neurochemistry, 96 (3), 825-832.
    • (2006) Journal of Neurochemistry , vol.96 , Issue.3 , pp. 825-832
    • Wang, J.1    Markesbery, W.R.2    Lovell, M.A.3
  • 133
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • Markesbery, W.R., Kryscio, R.J., Lovell, M.A. and Morrow, J.D. (2005) Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Annals of Neurology, 58 (5), 730-735.
    • (2005) Annals of Neurology , vol.58 , Issue.5 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 134
    • 8844285984 scopus 로고    scopus 로고
    • Mouse models of Alzheimer's disease: insight into treatment
    • German, D.C. and Eisch, A.J. (2004) Mouse models of Alzheimer's disease: insight into treatment. Reviews in the Neurosciences, 15 (5), 353-369.
    • (2004) Reviews in the Neurosciences , vol.15 , Issue.5 , pp. 353-369
    • German, D.C.1    Eisch, A.J.2
  • 135
    • 0034551780 scopus 로고    scopus 로고
    • Presenilin-1 P264L knock-in mutation: differential effects on abeta production amyloid deposition, and neuronal vulnerability
    • Siman, R., Reaume, A.G., Savage, M.J., Trusko, S., Lin, Y.G., Scott, R.W. and Flood, D.G. (2000) Presenilin-1 P264L knock-in mutation: differential effects on abeta production amyloid deposition, and neuronal vulnerability. Journal of Neuroscience, 20 (23), 8717-8726.
    • (2000) Journal of Neuroscience , vol.20 , Issue.23 , pp. 8717-8726
    • Siman, R.1    Reaume, A.G.2    Savage, M.J.3    Trusko, S.4    Lin, Y.G.5    Scott, R.W.6    Flood, D.G.7
  • 136
    • 13644268449 scopus 로고    scopus 로고
    • Changed conformation of mutant Tau-P301L underlies the moribund tauopathy absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice
    • Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Van Haesendonck, C., Borghgraef, P. and Van Leuven, F. (2005) Changed conformation of mutant Tau-P301L underlies the moribund tauopathy absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice. The Journal of Biological Chemistry, 280 (5), 3963-3973.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3963-3973
    • Terwel, D.1    Lasrado, R.2    Snauwaert, J.3    Vandeweert, E.4    Van Haesendonck, C.5    Borghgraef, P.6    Van Leuven, F.7
  • 137
    • 1642301524 scopus 로고    scopus 로고
    • Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse a syndrome that emanates from dysfunctional ubiquitin carboxyl-terminal hydrolase L-1, reveals oxidation of key proteins
    • Castegna, A., Thongboonkerd, V., Klein, J., Lynn, B.C., Wang, Y.L., Osaka, H., Wada, K. and Butterfield, D.A. (2004) Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse a syndrome that emanates from dysfunctional ubiquitin carboxyl-terminal hydrolase L-1, reveals oxidation of key proteins. Journal of Neurochemistry, 88 (6), 1540-1546.
    • (2004) Journal of Neurochemistry , vol.88 , Issue.6 , pp. 1540-1546
    • Castegna, A.1    Thongboonkerd, V.2    Klein, J.3    Lynn, B.C.4    Wang, Y.L.5    Osaka, H.6    Wada, K.7    Butterfield, D.A.8
  • 138
    • 16444385872 scopus 로고    scopus 로고
    • Gamma-glutamylcysteine ethyl ester protection of proteins from Abeta(1-42)-mediated oxidative stress in neuronal cell culture: a proteomics approach
    • Boyd-Kimball, D., Sultana, R., Poon, H.F., Mohmmad-Abdul, H., Lynn, B.C., Klein, J.B. and Butterfield, D.A. (2005) Gamma-glutamylcysteine ethyl ester protection of proteins from Abeta(1-42)-mediated oxidative stress in neuronal cell culture: a proteomics approach. Journal of Neuroscience Research, 79 (5), 707-713.
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.5 , pp. 707-713
    • Boyd-Kimball, D.1    Sultana, R.2    Poon, H.F.3    Mohmmad-Abdul, H.4    Lynn, B.C.5    Klein, J.B.6    Butterfield, D.A.7
  • 140
    • 31944446983 scopus 로고    scopus 로고
    • The glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function
    • Dhar-Chowdhury, P., Harrell, M.D., Han, S.Y., Jankowska, D., Parachuru, L., Morrissey, A., Srivastava, S., Liu, W., Malester, B., Yoshida, H. and Coetzee, W.A. (2005) The glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function. Journal of Biological Chemistry, 280 (46), 38464-38470.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38464-38470
    • Dhar-Chowdhury, P.1    Harrell, M.D.2    Han, S.Y.3    Jankowska, D.4    Parachuru, L.5    Morrissey, A.6    Srivastava, S.7    Liu, W.8    Malester, B.9    Yoshida, H.10    Coetzee, W.A.11
  • 141
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover, M.A. (1997) Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. Journal of Cellular Biochemistry, 66 (2), 133-140.
    • (1997) Journal of Cellular Biochemistry , vol.66 , Issue.2 , pp. 133-140
    • Sirover, M.A.1
  • 143
  • 145
    • 0030896788 scopus 로고    scopus 로고
    • Characteristics of age-related behavioral changes in senescence-accelerated mouse SAMP8 and SAMP10
    • Miyamoto, M. (1997) Characteristics of age-related behavioral changes in senescence-accelerated mouse SAMP8 and SAMP10. Experimental Gerontology, 32 (1-2), 139-148.
    • (1997) Experimental Gerontology , vol.32 , Issue.1-2 , pp. 139-148
    • Miyamoto, M.1
  • 146
    • 0030896787 scopus 로고    scopus 로고
    • Senescence-accelerated mouse (SAM): a novel murine model of senescence
    • Takeda, T., Hosokawa, M. and Higuchi, K. (1997) Senescence-accelerated mouse (SAM): a novel murine model of senescence. Experimental Gerontology, 32 (1-2), 105-109.
    • (1997) Experimental Gerontology , vol.32 , Issue.1-2 , pp. 105-109
    • Takeda, T.1    Hosokawa, M.2    Higuchi, K.3
  • 148
    • 0034867485 scopus 로고    scopus 로고
    • Site-directed antisense oligonucleotide decreases the expression ofamyloid precursor protein and reverses deficits in learning and memory in aged SAMP8 mice
    • Kumar, V.B., Farr, S.A., Flood, J.F., Kamlesh, V., Franko, M., Banks, W.A. and Morley, J.E. (2000) Site-directed antisense oligonucleotide decreases the expression ofamyloid precursor protein and reverses deficits in learning and memory in aged SAMP8 mice. Peptides, 21 (12), 1769-1775.
    • (2000) Peptides , vol.21 , Issue.12 , pp. 1769-1775
    • Kumar, V.B.1    Farr, S.A.2    Flood, J.F.3    Kamlesh, V.4    Franko, M.5    Banks, W.A.6    Morley, J.E.7
  • 149
    • 0034531444 scopus 로고    scopus 로고
    • Beta-amyloid precursor polypeptide in SAMP8 mice affects learning and memory
    • Morley, J.E., Kumar, V.B., Bernardo, A.E., Farr, S.A., Uezu, K., Tumosa, N. and Flood, J.F. (2000) Beta-amyloid precursor polypeptide in SAMP8 mice affects learning and memory. Peptides, 21 (12), 1761-1767.
    • (2000) Peptides , vol.21 , Issue.12 , pp. 1761-1767
    • Morley, J.E.1    Kumar, V.B.2    Bernardo, A.E.3    Farr, S.A.4    Uezu, K.5    Tumosa, N.6    Flood, J.F.7
  • 151
    • 0032566721 scopus 로고    scopus 로고
    • Increased mitochondrial DNA deletion in the brain of SAMP8 a mouse model for spontaneous oxidative stress brain
    • Fujibayashi, Y., Yamamoto, S., Waki, A., Konishi, J. and Yonekura, Y. (1998) Increased mitochondrial DNA deletion in the brain of SAMP8 a mouse model for spontaneous oxidative stress brain. Neuroscience Letters, 254 (2), 109-112.
    • (1998) Neuroscience Letters , vol.254 , Issue.2 , pp. 109-112
    • Fujibayashi, Y.1    Yamamoto, S.2    Waki, A.3    Konishi, J.4    Yonekura, Y.5
  • 153
    • 0035015218 scopus 로고    scopus 로고
    • Delivery across the blood-brain barrier of antisense directed against amyloid beta: reversal of learning and memory deficits in mice overexpressing amyloid precursor protein
    • Banks, W.A., Farr, S.A., Butt, W., Kumar, V.B., Franko, M.W. and Morley, J.E. (2001) Delivery across the blood-brain barrier of antisense directed against amyloid beta: reversal of learning and memory deficits in mice overexpressing amyloid precursor protein. Journal of Pharmacology and Experimental Therapeutics, 297 (3), 1113-1121.
    • (2001) Journal of Pharmacology and Experimental Therapeutics , vol.297 , Issue.3 , pp. 1113-1121
    • Banks, W.A.1    Farr, S.A.2    Butt, W.3    Kumar, V.B.4    Franko, M.W.5    Morley, J.E.6
  • 154
    • 0141867783 scopus 로고    scopus 로고
    • Efflux of human and mouse amyloid beta proteins 1-40 and 1-42 from brain: impairment in a mouse model of Alzheimers disease
    • Banks, W.A., Robinson, S.M., Verma, S. and Morley, J.E. (2003) Efflux of human and mouse amyloid beta proteins 1-40 and 1-42 from brain: impairment in a mouse model of Alzheimers disease. Neuroscience, 121 (2), 487-492.
    • (2003) Neuroscience , vol.121 , Issue.2 , pp. 487-492
    • Banks, W.A.1    Robinson, S.M.2    Verma, S.3    Morley, J.E.4
  • 155
    • 3242715959 scopus 로고    scopus 로고
    • Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice
    • Poon, H.F., Joshi, G., Sultana, R., Farr, S.A., Banks, W.A., Morley, J.E., Calabrese, V. and Butterfield, D.A. (2004) Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice. Brain Research, 1018 (1), 86-96.
    • (2004) Brain Research , vol.1018 , Issue.1 , pp. 86-96
    • Poon, H.F.1    Joshi, G.2    Sultana, R.3    Farr, S.A.4    Banks, W.A.5    Morley, J.E.6    Calabrese, V.7    Butterfield, D.A.8
  • 156
    • 0034674343 scopus 로고    scopus 로고
    • Identification of age-dependent changes in expression of senescence-accelerated mouse (SAMP8) hippocampal proteins by expression array analysis
    • Kumar, V.B., Franko, M.W., Farr, S.A., Armbrecht, H.J. and Morley, J.E. (2000) Identification of age-dependent changes in expression of senescence-accelerated mouse (SAMP8) hippocampal proteins by expression array analysis. Biochemical and Biophysical Research Communications, 272 (3), 657-661.
    • (2000) Biochemical and Biophysical Research Communications , vol.272 , Issue.3 , pp. 657-661
    • Kumar, V.B.1    Franko, M.W.2    Farr, S.A.3    Armbrecht, H.J.4    Morley, J.E.5
  • 157
    • 2942659505 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain
    • Poon, H.F., Castegna, A., Farr, S.A., Thongboonkerd, V., Lynn, B.C., Banks, W.A., Morley, J.E., Klein, J.B. and Butterfield, D.A. (2004) Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain. Neuroscience, 126 (4), 915-926.
    • (2004) Neuroscience , vol.126 , Issue.4 , pp. 915-926
    • Poon, H.F.1    Castegna, A.2    Farr, S.A.3    Thongboonkerd, V.4    Lynn, B.C.5    Banks, W.A.6    Morley, J.E.7    Klein, J.B.8    Butterfield, D.A.9
  • 158
    • 0033603608 scopus 로고    scopus 로고
    • Alzheimer's disease-related gene expression in the brain of senescence accelerated mouse
    • Wei, X., Zhang, Y. and Zhou, J. (1999) Alzheimer's disease-related gene expression in the brain of senescence accelerated mouse. Neuroscience Letters, 268 (3), 139-142.
    • (1999) Neuroscience Letters , vol.268 , Issue.3 , pp. 139-142
    • Wei, X.1    Zhang, Y.2    Zhou, J.3
  • 159
    • 0032832117 scopus 로고    scopus 로고
    • Differential display and cloning of the hippocampal gene mRNas in senescence accelerated mouse
    • Wei, X., Zhang, Y. and Zhou, J. (1999) Differential display and cloning of the hippocampal gene mRNas in senescence accelerated mouse. Neuroscience Letters, 275 (1), 17-20.
    • (1999) Neuroscience Letters , vol.275 , Issue.1 , pp. 17-20
    • Wei, X.1    Zhang, Y.2    Zhou, J.3
  • 160
    • 0033543584 scopus 로고    scopus 로고
    • Changes in membrane fatty acids and delta-9 desaturase in senescence accelerated (SAMP8) mouse hippocampus with aging
    • Kumar, V.B., Vyas, K., Buddhiraju, M., Alshaher, M., Flood, J.F. and Morley, J.E. (1999) Changes in membrane fatty acids and delta-9 desaturase in senescence accelerated (SAMP8) mouse hippocampus with aging. Life Sciences, 65 (16), 1657-1662.
    • (1999) Life Sciences , vol.65 , Issue.16 , pp. 1657-1662
    • Kumar, V.B.1    Vyas, K.2    Buddhiraju, M.3    Alshaher, M.4    Flood, J.F.5    Morley, J.E.6
  • 161
    • 0036252301 scopus 로고    scopus 로고
    • Melatonin reduces oxidative damage ofneural lipids and proteins in senescence-accelerated mouse
    • Okatani, Y., Wakatsuki, A., Reiter, R.J. and Miyahara, Y. (2002) Melatonin reduces oxidative damage ofneural lipids and proteins in senescence-accelerated mouse. Neurobiology of Aging, 23 (4), 639-644.
    • (2002) Neurobiology of Aging , vol.23 , Issue.4 , pp. 639-644
    • Okatani, Y.1    Wakatsuki, A.2    Reiter, R.J.3    Miyahara, Y.4
  • 162
    • 0030032553 scopus 로고    scopus 로고
    • Early and transient increase in oxidative stress in the cerebral cortex of senescence-accelerated mouse
    • Sato, E., Oda, N., Ozaki, N., Hashimoto, S., Kurokawa, T. and Ishibashi, S. (1996) Early and transient increase in oxidative stress in the cerebral cortex of senescence-accelerated mouse. Mechanisms of Ageing and Development, 86 (2), 105-114.
    • (1996) Mechanisms of Ageing and Development , vol.86 , Issue.2 , pp. 105-114
    • Sato, E.1    Oda, N.2    Ozaki, N.3    Hashimoto, S.4    Kurokawa, T.5    Ishibashi, S.6
  • 163
    • 0030590226 scopus 로고    scopus 로고
    • Evidence that glucose metabolism is decreased in the cerebrum of aged female senescence-accelerated mouse: possible involvement of a low hexokinase activity
    • Kurokawa, T., Sato, E., Inoue, A. and Ishibashi, S. (1996) Evidence that glucose metabolism is decreased in the cerebrum of aged female senescence-accelerated mouse: possible involvement of a low hexokinase activity. Neuroscience Letters, 214 (1), 45-48.
    • (1996) Neuroscience Letters , vol.214 , Issue.1 , pp. 45-48
    • Kurokawa, T.1    Sato, E.2    Inoue, A.3    Ishibashi, S.4
  • 164
    • 0032199904 scopus 로고    scopus 로고
    • Studies on aging through analysis of the glucose metabolism related to the ATP-production of the senescence accelerated mouse (SAM)
    • Shimano, Y. (1998) Studies on aging through analysis of the glucose metabolism related to the ATP-production of the senescence accelerated mouse (SAM). Hokkaido Igaku Zasshi, 73 (6), 557-569.
    • (1998) Hokkaido Igaku Zasshi , vol.73 , Issue.6 , pp. 557-569
    • Shimano, Y.1
  • 165
    • 0036293375 scopus 로고    scopus 로고
    • Intracellular deposition microtubule destabilization, and transport failure: an "early" pathogenic cascade leading to synaptic decline
    • Bendiske, J., Caba, E., Brown, Q.B. and Bahr, B.A. (2002) Intracellular deposition microtubule destabilization, and transport failure: an "early" pathogenic cascade leading to synaptic decline. Journal of Neuropathology and Experimental Neurology, 61 (7), 640-650.
    • (2002) Journal of Neuropathology and Experimental Neurology , vol.61 , Issue.7 , pp. 640-650
    • Bendiske, J.1    Caba, E.2    Brown, Q.B.3    Bahr, B.A.4
  • 166
    • 0035830408 scopus 로고    scopus 로고
    • Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease
    • Masliah, E., Mallory, M., Alford, M., DeTeresa, R., Hansen, L.A., McKeel, D.W., Jr and Morris, J.C. (2001) Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease. Neurology, 56 (1), 127-129.
    • (2001) Neurology , vol.56 , Issue.1 , pp. 127-129
    • Masliah, E.1    Mallory, M.2    Alford, M.3    DeTeresa, R.4    Hansen, L.A.5    McKeel Jr., D.W.6    Morris, J.C.7
  • 167
    • 33747760358 scopus 로고    scopus 로고
    • Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
    • Scheff, S.W., Price, D.A., Schmitt, F.A. and Mufson, E.J. (2005) Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment. Neurobiology of Aging. 27 (10), 1372-1384.
    • (2005) Neurobiology of Aging , vol.27 , Issue.10 , pp. 1372-1384
    • Scheff, S.W.1    Price, D.A.2    Schmitt, F.A.3    Mufson, E.J.4
  • 168
    • 0029942872 scopus 로고    scopus 로고
    • Patterns of synaptic and nerve cell pathology in Alzheimer's disease
    • Lassmann, H. (1996) Patterns of synaptic and nerve cell pathology in Alzheimer's disease. Behavioural Brain Research, 78 (1), 9-14.
    • (1996) Behavioural Brain Research , vol.78 , Issue.1 , pp. 9-14
    • Lassmann, H.1
  • 170
    • 15944386705 scopus 로고    scopus 로고
    • Membrane disordering effects of beta-amyloid peptides
    • Eckert, G.P., Wood, W.G. and Muller, W.E. (2005) Membrane disordering effects of beta-amyloid peptides. Subcellular Biochemistry, 38, 319-337.
    • (2005) Subcellular Biochemistry , vol.38 , pp. 319-337
    • Eckert, G.P.1    Wood, W.G.2    Muller, W.E.3
  • 171
    • 7244223228 scopus 로고    scopus 로고
    • Synaptic changes in Alzheimer's disease: increased amyloid-beta and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence
    • Gylys, K.H., Fein, J.A., Yang, F., Wiley, D.J., Miller, C.A. and Cole, G.M. (2004) Synaptic changes in Alzheimer's disease: increased amyloid-beta and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence. American Journal of Pathology, 165 (5), 1809-1817.
    • (2004) American Journal of Pathology , vol.165 , Issue.5 , pp. 1809-1817
    • Gylys, K.H.1    Fein, J.A.2    Yang, F.3    Wiley, D.J.4    Miller, C.A.5    Cole, G.M.6
  • 172
    • 0038053885 scopus 로고    scopus 로고
    • ATP synthesis driven by proton transport in F1F0-ATP synthase
    • Weber, J. and Senior, A.E. (2003) ATP synthesis driven by proton transport in F1F0-ATP synthase. FEBS Letters, 545 (1), 61-70.
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 61-70
    • Weber, J.1    Senior, A.E.2
  • 173
    • 0034738153 scopus 로고    scopus 로고
    • The rotary binding change mechanism of ATP synthases
    • Cross, R.L. (2000) The rotary binding change mechanism of ATP synthases. Biochimica et Biophysica Acta, 1458 (2-3), 270-275.
    • (2000) Biochimica et Biophysica Acta , vol.1458 , Issue.2-3 , pp. 270-275
    • Cross, R.L.1
  • 174
    • 0026806896 scopus 로고
    • H+ transport and coupling by the F0 sector of the ATP synthase: insights into the molecular mechanism of function
    • Fillingame, R.H. (1992) H+ transport and coupling by the F0 sector of the ATP synthase: insights into the molecular mechanism of function. Journal of Bioenergetics and Biomembranes, 24 (5), 485-491.
    • (1992) Journal of Bioenergetics and Biomembranes , vol.24 , Issue.5 , pp. 485-491
    • Fillingame, R.H.1
  • 175
    • 0842330579 scopus 로고    scopus 로고
    • How proton translocation across mitochondrial inner membranes drives the Fo rotor of ATP synthase
    • McCabe, M.G., Bourgain, R. and Maguire, D.J. (2003) How proton translocation across mitochondrial inner membranes drives the Fo rotor of ATP synthase. Advances in Experimental Medicine and Biology, 540, 133-138.
    • (2003) Advances in Experimental Medicine and Biology , vol.540 , pp. 133-138
    • McCabe, M.G.1    Bourgain, R.2    Maguire, D.J.3
  • 176
    • 0141497165 scopus 로고    scopus 로고
    • Molecular mechanisms of energy transduction in cells: engineering applications and biological implications
    • Nath, S. (2003) Molecular mechanisms of energy transduction in cells: engineering applications and biological implications. Advances in Biochemical Engineering/Biotechnology, 85, 125-180.
    • (2003) Advances in Biochemical Engineering/Biotechnology , vol.85 , pp. 125-180
    • Nath, S.1
  • 178
    • 0016683678 scopus 로고
    • Effects of increased mechanical work by isolated perfused rat heart during production or uptake of ketone bodies. Assessment of mitochondrial oxidized to reduced free nicotinamide-adenine dinucleotide ratios and oxaloacetate concentrations
    • Opie, L.H. and Owen, P. (1975) Effects of increased mechanical work by isolated perfused rat heart during production or uptake of ketone bodies. Assessment of mitochondrial oxidized to reduced free nicotinamide-adenine dinucleotide ratios and oxaloacetate concentrations. The Biochemical Journal, 148 (3), 403-415.
    • (1975) The Biochemical Journal , vol.148 , Issue.3 , pp. 403-415
    • Opie, L.H.1    Owen, P.2
  • 179
    • 0032460878 scopus 로고    scopus 로고
    • Morphological biochemical and behavioural changes induced by neuro-toxic and inflammatory insults to the nucleus basalis
    • Casamenti, F., Prosperi, C., Scali, C., Giovannelli, L. and Pepeu, G. (1998) Morphological biochemical and behavioural changes induced by neuro-toxic and inflammatory insults to the nucleus basalis. International Journal of Developmental Neuroscience, 16 (7-8), 705-714.
    • (1998) International Journal of Developmental Neuroscience , vol.16 , Issue.7-8 , pp. 705-714
    • Casamenti, F.1    Prosperi, C.2    Scali, C.3    Giovannelli, L.4    Pepeu, G.5
  • 181
    • 30344460006 scopus 로고    scopus 로고
    • Cholinergic challenge in Alzheimer patients and mild cognitive impairment differentially affects hippocampal activation-a pharmacological fMRI study
    • Goekoop, R., Scheltens, P., Barkhof, F. and Rombouts, S.A. (2006) Cholinergic challenge in Alzheimer patients and mild cognitive impairment differentially affects hippocampal activation-a pharmacological fMRI study. Brain, 129 (Pt 1), 141-157.
    • (2006) Brain , vol.129 , Issue.PT 1 , pp. 141-157
    • Goekoop, R.1    Scheltens, P.2    Barkhof, F.3    Rombouts, S.A.4
  • 182
    • 0027732875 scopus 로고
    • Excitotoxic lesions of basal forebrain cholinergic neurons: effects on learning memory and attention
    • Muir, J.L., Page, K.J., Sirinathsinghji, D.J., Robbins, T.W. and Everitt, B.J. (1993) Excitotoxic lesions of basal forebrain cholinergic neurons: effects on learning memory and attention. Behavioural Brain Research, 57 (2), 123-131.
    • (1993) Behavioural Brain Research , vol.57 , Issue.2 , pp. 123-131
    • Muir, J.L.1    Page, K.J.2    Sirinathsinghji, D.J.3    Robbins, T.W.4    Everitt, B.J.5
  • 183
    • 26244437738 scopus 로고    scopus 로고
    • Basal forebrain cholinergic dysfunction in Alzheimer's disease-interrelationship with beta-amyloid, inflammation and neuro-trophin signaling
    • Schliebs, R. (2005) Basal forebrain cholinergic dysfunction in Alzheimer's disease-interrelationship with beta-amyloid, inflammation and neuro-trophin signaling. Neurochemical Research, 30 (6-7), 895-908.
    • (2005) Neurochemical Research , vol.30 , Issue.6-7 , pp. 895-908
    • Schliebs, R.1
  • 184
    • 15744387176 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: implications for Alzheimer's disease
    • Boyd-Kimball, D., Sultana, R., Poon, H.F., Lynn, B.C., Casamenti, F., Pepeu, G., Klein, J.B. and Butterfield, D.A. (2005) ' Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: implications for Alzheimer's disease. Neuroscience, 132 (2), 313-324.
    • (2005) Neuroscience , vol.132 , Issue.2 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Poon, H.F.3    Lynn, B.C.4    Casamenti, F.5    Pepeu, G.6    Klein, J.B.7    Butterfield, D.A.8
  • 185
    • 0036968944 scopus 로고    scopus 로고
    • Beta-amyloid-induced inflammation and cholinergic hypofunction in the rat brain in vivo: involvement of the p38MAPK pathway
    • Giovannini, M.G., Scali, C., Prosperi, C., Bellucci, A., Vannucchi, M.G., Rosi, S., Pepeu, G. and Casamenti, F. (2002) Beta-amyloid-induced inflammation and cholinergic hypofunction in the rat brain in vivo: involvement of the p38MAPK pathway. Neurobiology of Disease, 11 (2), 257-274.
    • (2002) Neurobiology of Disease , vol.11 , Issue.2 , pp. 257-274
    • Giovannini, M.G.1    Scali, C.2    Prosperi, C.3    Bellucci, A.4    Vannucchi, M.G.5    Rosi, S.6    Pepeu, G.7    Casamenti, F.8
  • 186
    • 33646517324 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of differential protein expression and oxidative modification ofspecific proteins in the brains of old mice
    • Poon, H.F., Vaishnav, R.A., Getchell, T.V., Getchell, M.L. and Butterfield, D.A. (2006) Quantitative proteomics analysis of differential protein expression and oxidative modification ofspecific proteins in the brains of old mice. Neurobiology of Aging, 27 (7), 1010-1019.
    • (2006) Neurobiology of Aging , vol.27 , Issue.7 , pp. 1010-1019
    • Poon, H.F.1    Vaishnav, R.A.2    Getchell, T.V.3    Getchell, M.L.4    Butterfield, D.A.5
  • 187
    • 0035107082 scopus 로고    scopus 로고
    • A comparison of medial and lateral temporal lobe atrophy in dementia with Lewy bodies and Alzheimer's disease: magnetic resonance imaging volumetric study
    • Barber, R., McKeith, I.G., Ballard, C., Gholkar, A. and O'Brien, J.T. (2001) A comparison of medial and lateral temporal lobe atrophy in dementia with Lewy bodies and Alzheimer's disease: magnetic resonance imaging volumetric study. Dementia and Geriatric Cognitive Disorders, 12 (3), 198-205.
    • (2001) Dementia and Geriatric Cognitive Disorders , vol.12 , Issue.3 , pp. 198-205
    • Barber, R.1    McKeith, I.G.2    Ballard, C.3    Gholkar, A.4    O'Brien, J.T.5
  • 189
    • 23944459634 scopus 로고    scopus 로고
    • Comparison of gray matter and metabolic reduction in mild Alzheimer's disease using FDG-PET and voxel-based morphometric MR studies
    • Ishii, K., Sasaki, H., Kono, A.K., Miyamoto, N., Fukuda, T. and Mori, E. (2005) Comparison of gray matter and metabolic reduction in mild Alzheimer's disease using FDG-PET and voxel-based morphometric MR studies. European Journal of Nuclear Medicine and Molecular Imaging, 32 (8), 959-963.
    • (2005) European Journal of Nuclear Medicine and Molecular Imaging , vol.32 , Issue.8 , pp. 959-963
    • Ishii, K.1    Sasaki, H.2    Kono, A.K.3    Miyamoto, N.4    Fukuda, T.5    Mori, E.6
  • 190
    • 0035980919 scopus 로고    scopus 로고
    • Regulation of mammalian pyruvate dehydrogenase complex by phospho-rylation: complexity of multiple phosphorylation sites and kinases
    • Patel, M.S. and Korotchkina, L.G. (2001) Regulation of mammalian pyruvate dehydrogenase complex by phospho-rylation: complexity of multiple phosphorylation sites and kinases. Experimental and Molecular Medicine, 33 (4), 191-197.
    • (2001) Experimental and Molecular Medicine , vol.33 , Issue.4 , pp. 191-197
    • Patel, M.S.1    Korotchkina, L.G.2
  • 191
    • 0033819024 scopus 로고    scopus 로고
    • Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2, 6-bisphosphatase, acid phosphatase, and alkaline phosphatase
    • Jedrzejas, M.J. (2000) Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2, 6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Progress in Biophysics and Molecular Biology, 73 (2-4), 263-287.
    • (2000) Progress in Biophysics and Molecular Biology , vol.73 , Issue.2-4 , pp. 263-287
    • Jedrzejas, M.J.1
  • 192
    • 0037129849 scopus 로고    scopus 로고
    • Molecular characterization of phosphoglycerate mutase in archaea
    • van der Oost, J., Huynen, M.A. and Verhees, C.H. (2002) Molecular characterization of phosphoglycerate mutase in archaea. FEMS Microbiology Letters, 212 (1), 111-120.
    • (2002) FEMS Microbiology Letters , vol.212 , Issue.1 , pp. 111-120
    • van der Oost, J.1    Huynen, M.A.2    Verhees, C.H.3


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