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Volumn 132, Issue 2, 2005, Pages 313-324

Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid β-peptide (1-42) into rat brain: Implications for Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid peptide (1 42); Neurodegeneration; Oxidative stress; Proteomics

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; BETA SYNUCLEIN; GLUTAMATE AMMONIA LIGASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PHOSPHOGLYCERATE MUTASE; PYRUVATE DEHYDROGENASE; SODIUM CHLORIDE;

EID: 15744387176     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2004.12.022     Document Type: Article
Times cited : (155)

References (65)
  • 1
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 Connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex
    • A. Agarwal-Mawal, H.Y. Qureshi, P.W. Cafferty, Z. Yuan, D. Han, R. Lin, H.K. Paudel 14-3-3 Connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex J Biol Chem 278 2003 12722 12728
    • (2003) J Biol Chem , vol.278 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3    Yuan, Z.4    Han, D.5    Lin, R.6    Paudel, H.K.7
  • 3
    • 0032971621 scopus 로고    scopus 로고
    • The expression of several mitochondrial and nuclear genes encoding the subunits of electron transport chain enzyme complexes, cytochrome c oxidase, and NADH dehydrogenase in different brain regions in Alzheimer's disease brain
    • M.Y. Aksenov, H.M. Tucker, P. Nair, M.V. Askenova, D.A. Butterfield, S. Estus, W.R. Markesbery The expression of several mitochondrial and nuclear genes encoding the subunits of electron transport chain enzyme complexes, cytochrome c oxidase, and NADH dehydrogenase in different brain regions in Alzheimer's disease brain Neurochem Res 24 1999 767 774
    • (1999) Neurochem Res , vol.24 , pp. 767-774
    • Aksenov, M.Y.1    Tucker, H.M.2    Nair, P.3    Askenova, M.V.4    Butterfield, D.A.5    Estus, S.6    Markesbery, W.R.7
  • 4
    • 0025734299 scopus 로고
    • The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease
    • J.P. Blass, G.E. Gibson The role of oxidative abnormalities in the pathophysiology of Alzheimer's disease Rev Neurol 147 1991 513 525
    • (1991) Rev Neurol , vol.147 , pp. 513-525
    • Blass, J.P.1    Gibson, G.E.2
  • 6
    • 0035849483 scopus 로고    scopus 로고
    • CSF detection of the 14-3-3 protein in unselected patients with dementia
    • P.R. Burkhard, J.C. Sanchex, T. Landis, D.F. Hochstrasser CSF detection of the 14-3-3 protein in unselected patients with dementia Neurology 56 2001 1528 1533
    • (2001) Neurology , vol.56 , pp. 1528-1533
    • Burkhard, P.R.1    Sanchex, J.C.2    Landis, T.3    Hochstrasser, D.F.4
  • 7
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: Implications for neurodegeneration in Alzheimer's disease brain
    • D.A. Butterfield Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity implications for neurodegeneration in Alzheimer's disease brain Free Radic Res 36 2002 1307 1313
    • (2002) Free Radic Res , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 8
    • 0344824654 scopus 로고    scopus 로고
    • Amyloid beta-peptide [1-42]-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: Mechanisms and consequences
    • D.A. Butterfield Amyloid beta-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
  • 9
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: A new approach to study oxidative stress in Alzheimer's disease brain
    • D.A. Butterfield Proteomics a new approach to study oxidative stress in Alzheimer's disease brain Brain Res 1000 2004 1 7
    • (2004) Brain Res , vol.1000 , pp. 1-7
    • Butterfield, D.A.1
  • 10
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • D.A. Butterfield, J. Drake, C. Pocernich, A. Castegna Evidence of oxidative damage in Alzheimer's disease brain central role for amyloid beta-peptide Trends Mol Med 7 2001 548 554
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 11
    • 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
    • D.A. Butterfield, C.M. Lauderback Lipid peroxidation and protein oxidation in Alzheimer's disease brain potential causes and consequences involving amyloid beta-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
  • 13
    • 0032587025 scopus 로고    scopus 로고
    • Interleukin-1 β activates forebrain glial cells and increases nitric oxide production and cortical glutamate and GABA release in vivo: Implication for Alzheimer's disease
    • F. Casamenti, C. Prosperi, C. Scali, L. Giovanelli, M.A. Colivicchi, M.S. Faussone-Pelligrini, G. Pepeu Interleukin-1 β activates forebrain glial cells and increases nitric oxide production and cortical glutamate and GABA release in vivo implication for Alzheimer's disease Neuroscience 91 1999 831 842
    • (1999) Neuroscience , vol.91 , pp. 831-842
    • Casamenti, F.1    Prosperi, C.2    Scali, C.3    Giovanelli, L.4    Colivicchi, M.A.5    Faussone-Pelligrini, M.S.6    Pepeu, G.7
  • 14
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain part I: Creatine kinase BB, glutamine synthetase, and ubiquitin carboxy-terminal hydrolase L-1
    • A. Castegna, M. Aksenov, M. Aksenova, V. Thongboonkerd, J.B. Klein, W.M. Pierce, R. Booze, W.R. Marksbery, D.A. Butterfield Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain part I creatine kinase BB, glutamine synthetase, and ubiquitin carboxy-terminal hydrolase L-1 Free Rad Biol Med 33 2002 562 571
    • (2002) Free Rad Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Marksbery, W.R.8    Butterfield, D.A.9
  • 15
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase-related protein 2, α-enolase, and heat shock cognate 71
    • A. Castegna, M. Aksenov, Thongboonkerd, J.B. Klein, W.M. Pierce, R. Booze, W.R. Markesbery, D.A. Butterfield Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase- related protein 2, α-enolase, and heat shock cognate 71 J Neurochem 82 2002 1524 1532
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 16
    • 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
    • A. Castegna, V. Thongboonkerd, J. Klein, B.C. Lynn, Y.L. Wang, H. Osaka, K. Wada, D.A. Butterfield 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 J Neurochem 88 2004 1540 1546
    • (2004) J Neurochem , vol.88 , 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
  • 18
    • 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
    • J. Choi, A.I. Levey, S.T. Weintraub, H.D. Rees, M. Gearing, L.-S. Chin, L. Li Oxidative modifications and down regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases J Biol Chem 279 2004 13256 13264
    • (2004) J Biol Chem , vol.279 , 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
  • 20
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • M.K. Dougherty, D.K. Morrison Unlocking the code of 14-3-3 J Cell Sci 117 2004 1875 1884
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 21
    • 12244281810 scopus 로고    scopus 로고
    • Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1-42) in a transgenic Caenorhabditis elegans model
    • J. Drake, C.D. Link, D.A. Butterfield Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1-42) in a transgenic Caenorhabditis elegans model Neurobiol Aging 24 2003 415 420
    • (2003) Neurobiol Aging , vol.24 , pp. 415-420
    • Drake, J.1    Link, C.D.2    Butterfield, D.A.3
  • 22
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Rad Biol Med 11 1991 81 128
    • (1991) Free Rad Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 23
    • 0032585827 scopus 로고    scopus 로고
    • Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome
    • M. Fountoulakis, N. Cairns, G. Lubec Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome J Neural Transm Suppl 57 1999 323 335
    • (1999) J Neural Transm Suppl , vol.57 , pp. 323-335
    • Fountoulakis, M.1    Cairns, N.2    Lubec, G.3
  • 24
    • 0026070054 scopus 로고
    • Effects of injection of Alzheimer β-amyloid cores in rat brain
    • S.A. Frautschy, A. Baird, G.M. Cole Effects of injection of Alzheimer β-amyloid cores in rat brain Proc Natl Acad Sci USA 88 1991 8362 8366
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8362-8366
    • Frautschy, S.A.1    Baird, A.2    Cole, G.M.3
  • 25
    • 0036318769 scopus 로고    scopus 로고
    • The cholinergic pathology in Alzheimer's disease: Discrepancies between clinical experience and pathophysiological findings
    • L. Frölich The cholinergic pathology in Alzheimer's disease discrepancies between clinical experience and pathophysiological findings J Neural Transm 109 2002 1003 1014
    • (2002) J Neural Transm , vol.109 , pp. 1003-1014
    • Frölich, L.1
  • 26
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • G.E. Gibson, K.F. Sheu, J.P. Blass, A. Baker, K.C. Carlson, B. Harding, P. Perrino Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease Arch Neurol 45 1988 836 840
    • (1988) Arch Neurol , vol.45 , pp. 836-840
    • Gibson, G.E.1    Sheu, K.F.2    Blass, J.P.3    Baker, A.4    Carlson, K.C.5    Harding, B.6    Perrino, P.7
  • 27
    • 0032551649 scopus 로고    scopus 로고
    • Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain
    • L. Giovannelli, C. Scali, M.S. Faussone-Pelligrini, G. Pepeu, F. Casamenti Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain Neuroscience 87 1998 349 357
    • (1998) Neuroscience , vol.87 , pp. 349-357
    • Giovannelli, L.1    Scali, C.2    Faussone-Pelligrini, M.S.3    Pepeu, G.4    Casamenti, F.5
  • 29
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling
    • C.A. Grimes, R.S. Jope The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling Prog Neurobiol 65 2001 391 426
    • (2001) Prog Neurobiol , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 30
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3 Zeta is an effector of tau protein phosphorylation
    • M. Hashiguchi, K. Sobue, H.K. Paudel 14-3-3 Zeta is an effector of tau protein phosphorylation J Biol Chem 275 2000 25247 25254
    • (2000) J Biol Chem , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 31
    • 2542499831 scopus 로고    scopus 로고
    • β-Synuclein regulateds Akt activity in neuronal cells: A possible mechanism for neuroprotection in Parkinson's disease
    • published online March 16 2004.
    • Hashimoto M, Baron P, Ho G, Takenouchi T, Rockenstein E, Crews L, Masliah E (2004) β-Synuclein regulateds Akt activity in neuronal cells: a possible mechanism for neuroprotection in Parkinson's disease. J Biol Chem, published online March 16 2004.
    • (2004) J Biol Chem
    • Hashimoto, M.1    Baron, P.2    Ho, G.3    Takenouchi, T.4    Rockenstein, E.5    Crews, L.6    Masliah, E.7
  • 33
    • 1242337344 scopus 로고    scopus 로고
    • Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers
    • F. Hernández, R. Cuadros, J. Avila Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers Neurosci Lett 357 2004 143 146
    • (2004) Neurosci Lett , vol.357 , pp. 143-146
    • Hernández, F.1    Cuadros, R.2    Avila, J.3
  • 34
    • 0019142890 scopus 로고
    • Glycolytic enzymes from human autoptic brain cortex: Normal aged and demented cases
    • P. Iwangoff, R. Armbruster, A. Enz, W. Meier-Ruge Glycolytic enzymes from human autoptic brain cortex normal aged and demented cases Mech Ageing Dev 14 1980 203 209
    • (1980) Mech Ageing Dev , vol.14 , pp. 203-209
    • Iwangoff, P.1    Armbruster, R.2    Enz, A.3    Meier-Ruge, W.4
  • 35
    • 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
    • C.M. Lauderback, J.M. Hackett, F.F. Huang, J.N. Keller, L.I. Szweda, W.R. Markesbery, D.A. Butterfield 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 J Neurochem 78 2001 413 416
    • (2001) J Neurochem , vol.78 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3    Keller, J.N.4    Szweda, L.I.5    Markesbery, W.R.6    Butterfield, D.A.7
  • 37
  • 38
    • 0037067993 scopus 로고    scopus 로고
    • Differential localization of α-, β-, and γ-synucleins in the rat CNS
    • J.Y. Li, P. Henning Jensen, A. Dahlstrom Differential localization of α-, β-, and γ-synucleins in the rat CNS Neuroscience 113 2002 463 478
    • (2002) Neuroscience , vol.113 , pp. 463-478
    • Li, J.Y.1    Henning Jensen, P.2    Dahlstrom, A.3
  • 39
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • K.M. Lin, B. Lin, I.Y. Lian, R. Mestril, I.E. Scheffler, W.H. Dillmann Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation Circulation 103 2001 1787 1792
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 40
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • M.A. Lovell, C. Xie, W.R. Markesbery Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures Neurobiol Aging 22 2001 187 194
    • (2001) Neurobiol Aging , vol.22 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 41
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • R.J. Mark, M.A. Lovell, W.R. Markesbery, K. Uchida, M.P. Mattson A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide J Neurochem 68 1997 255 264
    • (1997) J Neurochem , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 42
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • W.R. Markesbery, M.A. Lovell Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease Neurobiol Aging 19 1998 33 36
    • (1998) Neurobiol Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 43
    • 0029811226 scopus 로고    scopus 로고
    • Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease
    • E. Masliah, M. Alford, R. DeTeresa, M. Mallory, L. Hansen Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease Ann Neurol 40 1996 759 766
    • (1996) Ann Neurol , vol.40 , pp. 759-766
    • Masliah, E.1    Alford, M.2    Deteresa, R.3    Mallory, M.4    Hansen, L.5
  • 45
    • 0035145627 scopus 로고    scopus 로고
    • Reduction of glyceraldehydes-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts
    • J.L. Mazzola, M.A. Sirover Reduction of glyceraldehydes-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts J Neurochem 76 2001 442 449
    • (2001) J Neurochem , vol.76 , pp. 442-449
    • Mazzola, J.L.1    Sirover, M.A.2
  • 46
    • 0034518249 scopus 로고    scopus 로고
    • Glucose regulation and brain aging
    • C. Messier, M. Gagnon Glucose regulation and brain aging J Nutr Health Aging 4 2000 208 213
    • (2000) J Nutr Health Aging , vol.4 , pp. 208-213
    • Messier, C.1    Gagnon, M.2
  • 48
    • 0027429156 scopus 로고
    • A new brain-specific 14 kd protein is a phosphoprotein: Its complete amino acid sequence and evidence for phosphorylation
    • S. Nakajo, K. Tsukada, K. Omata, K. Nakamura A new brain-specific 14 kd protein is a phosphoprotein its complete amino acid sequence and evidence for phosphorylation Eur J Biochem 217 1993 1057 1063
    • (1993) Eur J Biochem , vol.217 , pp. 1057-1063
    • Nakajo, S.1    Tsukada, K.2    Omata, K.3    Nakamura, K.4
  • 51
    • 0034620476 scopus 로고    scopus 로고
    • Cerebrospinal fluid pyruvate levels in Alzheimer's disease and vascular dementia
    • L. Parnetti, G.P. Reboldi, V. Gallai Cerebrospinal fluid pyruvate levels in Alzheimer's disease and vascular dementia Neurology 54 2000 735 737
    • (2000) Neurology , vol.54 , pp. 735-737
    • Parnetti, L.1    Reboldi, G.P.2    Gallai, V.3
  • 53
    • 1342306400 scopus 로고    scopus 로고
    • Acrolien inhibits NADH-linked mitochondrial enzyme activity: Implications for Alzheimer's disease
    • C.B. Pocernich, D.A. Butterfield Acrolien inhibits NADH-linked mitochondrial enzyme activity implications for Alzheimer's disease Neurotox Res 5 2003 515 520
    • (2003) Neurotox Res , vol.5 , pp. 515-520
    • Pocernich, C.B.1    Butterfield, D.A.2
  • 54
    • 0033859068 scopus 로고    scopus 로고
    • Contribution of neuroimaging in the diagnosis of Alzheimer's disease and other dementias
    • P. Scheltens, E.S.C. Korf Contribution of neuroimaging in the diagnosis of Alzheimer's disease and other dementias Curr Opin Neurol 13 2000 391 396
    • (2000) Curr Opin Neurol , vol.13 , pp. 391-396
    • Scheltens, P.1    Korf, E.S.C.2
  • 55
    • 0035656206 scopus 로고    scopus 로고
    • Proteomic analysis of the brain in Alzheimer's disease: Molecular phenotype of a complex disease process
    • S.J. Schonberger, P.F. Edgar, R. Kydd, R.L.M. Faull, G.J.S. Cooper Proteomic analysis of the brain in Alzheimer's disease molecular phenotype of a complex disease process Proteomics 1 2001 1519 1528
    • (2001) Proteomics , vol.1 , pp. 1519-1528
    • Schonberger, S.J.1    Edgar, P.F.2    Kydd, R.3    Faull, R.L.M.4    Cooper, G.J.S.5
  • 56
    • 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
  • 57
    • 0030746621 scopus 로고    scopus 로고
    • The lipid peroxidation product, 4-hydroxy-2-trans-nonenal, alters the conformation of cortical synaptosomal membrane protein
    • R. Subramaniam, F. Roediger, B. Jordan, M.P. Mattson, J.N. Keller, G. Waeg, D.A. Butterfield The lipid peroxidation product, 4-hydroxy-2-trans- nonenal, alters the conformation of cortical synaptosomal membrane protein J Neurochem 69 1997 1161 1169
    • (1997) J Neurochem , vol.69 , pp. 1161-1169
    • Subramaniam, R.1    Roediger, F.2    Jordan, B.3    Mattson, M.P.4    Keller, J.N.5    Waeg, G.6    Butterfield, D.A.7
  • 58
    • 0038724088 scopus 로고    scopus 로고
    • The 14-3-3 proteins: Gene, gene expression, and function
    • Y. Takahashi The 14-3-3 proteins gene, gene expression, and function Neurochem Res 28 2003 1265 1273
    • (2003) Neurochem Res , vol.28 , pp. 1265-1273
    • Takahashi, Y.1
  • 60
    • 0031797832 scopus 로고    scopus 로고
    • Glucose intolerance, cognitive impairment and Alzheimer's disease
    • M. Vanhanen, H. Soininen Glucose intolerance, cognitive impairment and Alzheimer's disease Curr Opin Neurol 11 1998 673 677
    • (1998) Curr Opin Neurol , vol.11 , pp. 673-677
    • Vanhanen, M.1    Soininen, H.2
  • 61
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • S. Varadarajan, S. Yatin, M. Aksenova, D.A. Butterfield Review Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity J Struct Biol 130 2000 184 208
    • (2000) J Struct Biol , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 62
    • 0019410162 scopus 로고
    • Alzheimer's disease: Evidence for selective loss of cholinergic neurons in the nucleus basalis
    • P.J. Whitehouse, D.L. Price, A.W. Clark, J.T. Coyle, M.R. Delong Alzheimer's disease evidence for selective loss of cholinergic neurons in the nucleus basalis Ann Neurol 10 1981 122 126
    • (1981) Ann Neurol , vol.10 , pp. 122-126
    • Whitehouse, P.J.1    Price, D.L.2    Clark, A.W.3    Coyle, J.T.4    Delong, M.R.5
  • 63
    • 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, 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
  • 64
    • 0033788416 scopus 로고    scopus 로고
    • Vitamin e prevents Alzheimer's amyloid beta-peptide (1-42)-induced protein oxidation and reactive oxygen species formation
    • S.M. Yatin, S. Varadarajan, D.A. Butterfield Vitamin E prevents Alzheimer's amyloid beta-peptide (1-42)-induced protein oxidation and reactive oxygen species formation J Alzheimer's Dis 2 2000 123 131
    • (2000) J Alzheimer's Dis , vol.2 , pp. 123-131
    • Yatin, S.M.1    Varadarajan, S.2    Butterfield, D.A.3
  • 65
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • B.C. Yoo, S.H. Kim, N. Cairns, M. Fountoulakis, G. Lubec Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease Biochem Biophys Res Commun 280 2001 249 258
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 249-258
    • Yoo, B.C.1    Kim, S.H.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5


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