메뉴 건너뛰기




Volumn 33, Issue SUPPL. 1, 2013, Pages

Oxidative modification of brain proteins in Alzheimer's disease: Perspective on future studies based on results of redox proteomics studies

Author keywords

Alzheimer's disease; lipid peroxidation; mild cognitive impairment; oxidative stress; protein carbonylation; protein nitration; redox proteomics

Indexed keywords

ALPHA 2 MACROGLOBULIN; ALPHA ACTIN; ALPHA ENOLASE; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; BETA ACTIN; BETA SECRETASE; CARBONATE DEHYDRATASE I; CARBONATE DEHYDRATASE II; CLATHRIN ASSEMBLY PROTEIN; CLUSTERIN; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; CREATINE KINASE BB; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GAMMA SECRETASE; GLUTAMATE AMMONIA LIGASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; MALATE DEHYDROGENASE; MITOGEN ACTIVATED PROTEIN KINASE 1; NEURON SPECIFIC ENOLASE; PEPTIDYLPROLYL ISOMERASE PIN1; PRESENILIN 1; PRESENILIN 2; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SYNTAXIN 1; TAU PROTEIN; UBIQUITIN THIOLESTERASE;

EID: 84872520228     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2012-129018     Document Type: Review
Times cited : (66)

References (76)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: Genes, proteins, and therapy. Physiol Rev 81, 741-766
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 66249141948 scopus 로고    scopus 로고
    • Alzheimer's disease genetics current status and future perspectives
    • Bertram L (2009) Alzheimer's disease genetics current status and future perspectives. Int Rev Neurobiol 84, 167-184
    • (2009) Int Rev Neurobiol , vol.84 , pp. 167-184
    • Bertram, L.1
  • 3
    • 77957730965 scopus 로고    scopus 로고
    • Genome-wide association studies in Alzheimer's disease
    • Bertram L,TanziRE(2009) Genome-wide association studies in Alzheimer's disease. Hum Mol Genet 18, R137-R145
    • (2009) Hum Mol Genet , vol.18
    • Bertram, L.1    Tanzi, R.E.2
  • 6
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid b-Protein and the genetics of Alzheimer's disease
    • Selkoe DJ (1996) Amyloid b-Protein and the genetics of Alzheimer's disease. J Biol Chem 271, 18295-18298
    • (1996) J Biol Chem , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 7
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid beta-Peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield DA, Boyd-Kimball D (2005) The critical role of methionine 35 in Alzheimer's amyloid beta-Peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim Biophys Acta 1703, 149-156
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 8
    • 84861470082 scopus 로고    scopus 로고
    • Methionine-35 of A 1-2 42): Importance for oxidative stress in Alzheimer disease
    • Butterfield DA, Sultana R (2011) Methionine-35 of A-(1-42): Importance for oxidative stress in Alzheimer disease. J Amino Acid 2011, 198430
    • (2011) J Amino Acid , vol.2011 , pp. 198430
    • Butterfield, D.A.1    Sultana, R.2
  • 9
    • 1842519391 scopus 로고    scopus 로고
    • Alzheimer's amyloid betapeptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide
    • Butterfield DA, Bush AI (2004) Alzheimer's amyloid betapeptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol Aging 25, 563-568
    • (2004) Neurobiol Aging , vol.25 , pp. 563-568
    • Butterfield, D.A.1    Bush, A.I.2
  • 10
    • 11144261790 scopus 로고    scopus 로고
    • Oxidatively modified GST and MRP1 in Alzheimer's disease brain: Implications for accumulation of reactive lipid peroxidation products
    • Sultana R, Butterfield DA (2004) Oxidatively modified GST and MRP1 in Alzheimer's disease brain: Implications for accumulation of reactive lipid peroxidation products. Neurochem Res 29, 2215-2220
    • (2004) Neurochem Res , vol.29 , pp. 2215-2220
    • Sultana, R.1    Butterfield, D.A.2
  • 11
    • 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 Abeta1-42
    • Lauderback CM, Hackett JM, Huang FF, Keller JN, Szweda LI, Markesbery WR, Butterfield DA (2001) The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-Nonenal in the Alzheimer's disease brain: The role of Abeta1-42. J Neurochem 78, 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
  • 12
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-Phosphate dehydrogenase (GAPDH) and Alzheimer disease: Many pathways to neurodegeneration
    • Butterfield DA, Hardas SS, Lange ML (2010) Oxidatively modified glyceraldehyde-3-Phosphate dehydrogenase (GAPDH) and Alzheimer disease: Many pathways to neurodegeneration. J Alzheimers Dis 20, 369-393
    • (2010) J Alzheimers Dis , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.3
  • 13
    • 14744281174 scopus 로고    scopus 로고
    • Neurotoxicity and oxidative stress in D1M-Substituted Alzheimer's A beta(1-42): Relevance to N-Terminal methionine chemistry in small model peptides
    • Boyd-Kimball D, Sultana R, Mohmmad-Abdul H, Butterfield DA (2005) Neurotoxicity and oxidative stress in D1M-Substituted Alzheimer's A beta(1-42): Relevance to N-Terminal methionine chemistry in small model peptides. Peptides 26, 665-673
    • (2005) Peptides , vol.26 , pp. 665-673
    • Boyd-Kimball, D.1    Sultana, R.2    Mohmmad-Abdul, H.3    Butterfield, D.A.4
  • 14
    • 12844260763 scopus 로고    scopus 로고
    • Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease
    • Schoneich C (2005) Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease. Biochim Biophys Acta 1703, 111-119
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 111-119
    • Schoneich, C.1
  • 15
    • 0032401643 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress are significantly elevated in Down syndrome
    • Jovanovic SV, Clements D, MacLeodK(1998) Biomarkers of oxidative stress are significantly elevated in Down syndrome. Free Radic Biol Med 25, 1044-1048
    • (1998) Free Radic Biol Med , vol.25 , pp. 1044-1048
    • Jovanovic, S.V.1    Clements D MacLeodK2
  • 17
    • 75949121583 scopus 로고    scopus 로고
    • Oxidative stress in the progression of Alzheimer disease in the frontal cortex
    • Ansari MA, Scheff SW(2010) Oxidative stress in the progression of Alzheimer disease in the frontal cortex. J Neuropathol Exp Neurol 69, 155-167
    • (2010) J Neuropathol Exp Neurol , vol.69 , pp. 155-167
    • Ansari, M.A.1    Scheff, S.W.2
  • 21
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • Markesbery WR, Kryscio RJ, Lovell MA,Morrow JD (2005) Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Ann Neurol 58, 730-735
    • (2005) Ann Neurol , vol.58 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 24
    • 2342420034 scopus 로고    scopus 로고
    • Lipid peroxidation and oxidative imbalance: Early functional events in Alzheimer's disease
    • Pratico D, Sung S (2004) Lipid peroxidation and oxidative imbalance: Early functional events in Alzheimer's disease. J Alzheimers Dis 6, 171-175
    • (2004) J Alzheimers Dis , vol.6 , pp. 171-175
    • Pratico, D.1    Sung, S.2
  • 25
    • 0036284936 scopus 로고    scopus 로고
    • Increase of brain oxidative stress in mild cognitive impairment: A possible predictor of Alzheimer disease
    • Pratico D, Clark CM, Liun F, Rokach J, Lee VY, Trojanowski JQ (2002) Increase of brain oxidative stress in mild cognitive impairment: A possible predictor of Alzheimer disease. Arch Neurol 59, 972-976
    • (2002) Arch Neurol , vol.59 , pp. 972-976
    • Pratico, D.1    Clark, C.M.2    Liun, F.3    Rokach, J.4    Lee, V.Y.5    Trojanowski, J.Q.6
  • 27
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield DA, Perluigi M, Sultana R (2006) Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics. Eur J Pharmacol 545, 39-50
    • (2006) Eur J Pharmacol , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 28
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-Peptide
    • Butterfield DA, Drake J, Pocernich C, Castegna A (2001) Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-Peptide. Trends Mol Med 7, 548-554
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 29
    • 34547102265 scopus 로고    scopus 로고
    • Roles of amyloid beta-Peptide-Associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment
    • Butterfield DA, Reed T, Newman SF, Sultana R (2007) Roles of amyloid beta-Peptide-Associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment. Free Radic Biol Med 43, 658-677
    • (2007) Free Radic Biol Med , vol.43 , pp. 658-677
    • Butterfield, D.A.1    Reed, T.2    Newman, S.F.3    Sultana, R.4
  • 30
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery WR (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med 23, 134-147
    • (1997) Free Radic Biol Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 32
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-Peptide (1-42
    • 325-330; discussion
    • Yatin SM, Varadarajan S, Link CD, Butterfield DA (1999) In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-Peptide (1-42). Neurobiol Aging 20, 325-330; discussion 339-342
    • (1999) Neurobiol Aging , vol.20 , pp. 339-342
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 33
    • 0031842223 scopus 로고    scopus 로고
    • Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies
    • Lyras L, Perry RH, Perry EK, Ince PG, Jenner A, Jenner P, Halliwell B (1998) Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia with Lewy bodies. J Neurochem 71, 302-312
    • (1998) J Neurochem , vol.71 , pp. 302-312
    • Lyras, L.1    Perry, R.H.2    Perry, E.K.3    Ince, P.G.4    Jenner, A.5    Jenner, P.6    Halliwell, B.7
  • 34
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta(1-42
    • Sultana R, Perluigi M, Butterfield DA (2006) Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta(1-42). J Chromatogr B Analyt Technol Biomed Life Sci 833, 3-11
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.833 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 35
    • 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 DA, Reed T, Perluigi M, De Marco C, Coccia R, Cini C, Sultana R (2006) Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-Nonenal, in brain from persons with mild cognitive impairment. Neurosci Lett 397, 170-173
    • (2006) Neurosci Lett , vol.397 , 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
  • 36
    • 38149087424 scopus 로고    scopus 로고
    • Oxidatively modified RNA in mild cognitive impairment
    • Lovell MA, Markesbery WR (2008) Oxidatively modified RNA in mild cognitive impairment. Neurobiol Dis 29, 169-175
    • (2008) Neurobiol Dis , vol.29 , pp. 169-175
    • Lovell, M.A.1    Markesbery, W.R.2
  • 37
    • 79951560784 scopus 로고    scopus 로고
    • Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer's disease: Insights into memory loss in MCI
    • Aluise CD, Robinson RA, Cai J, Pierce WM, Markesbery WR, Butterfield DA (2011) Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer's disease: Insights into memory loss in MCI. J Alzheimers Dis 23, 257-269
    • (2011) J Alzheimers Dis , vol.23 , pp. 257-269
    • Aluise, C.D.1    Robinson, R.A.2    Cai, J.3    Pierce, W.M.4    Markesbery, W.R.5    Butterfield, D.A.6
  • 39
    • 33847069643 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment
    • Butterfield DA, Gnjec A, Poon HF, Castegna A, Pierce WM, Klein JB, Martins RN (2006) Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment. J Alzheimers Dis 10, 391-397
    • (2006) J Alzheimers Dis , vol.10 , pp. 391-397
    • Butterfield, D.A.1    Gnjec, A.2    Poon, H.F.3    Castegna, A.4    Pierce, W.M.5    Klein, J.B.6    Martins, R.N.7
  • 41
    • 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 JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA (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 Radic Biol Med 33, 562-571
    • (2002) Free Radic Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 42
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinaserelated protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, AksenovM, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinaserelated protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82, 1524-1532
    • (2002) J Neurochem , vol.82 , 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
  • 45
    • 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 HF, Cai J, Pierce WM, Klein JB, Merchant M, Markesbery WR, Butterfield DA (2006) Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD. Neurobiol Aging 27, 1564-1576
    • (2006) Neurobiol Aging , vol.27 , 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
  • 46
    • 34548172399 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: A regional study
    • Sultana R, Reed T, Perluigi M, Coccia R, Pierce WM, Butterfield DA (2007) Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: A regional study. J Cell Mol Med 11, 839-851
    • (2007) J Cell Mol Med , vol.11 , pp. 839-851
    • Sultana, R.1    Reed, T.2    Perluigi, M.3    Coccia, R.4    Pierce, W.M.5    Butterfield, D.A.6
  • 47
    • 40849120274 scopus 로고    scopus 로고
    • Redox proteomic identification of 4-hydroxy-2-Nonenal-Modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease
    • Reed T, Perluigi M, Sultana R, Pierce WM, Klein JB, Turner DM, Coccia R, Markesbery WR, Butterfield DA (2008) Redox proteomic identification of 4-hydroxy-2-Nonenal-Modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease. Neurobiol Dis 30, 107-120
    • (2008) Neurobiol Dis , vol.30 , pp. 107-120
    • Reed, T.1    Perluigi, M.2    Sultana, R.3    Pierce, W.M.4    Klein, J.B.5    Turner, D.M.6    Coccia, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 49
    • 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 AI, Weintraub ST, Rees HD, Gearing M, Chin LS, Li L (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-Terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J Biol Chem 279, 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
  • 50
    • 1842634504 scopus 로고    scopus 로고
    • Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer's disease
    • Choi J, Forster MJ, McDonald SR, Weintraub ST, Carroll CA, Gracy RW (2004) Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer's disease. Free Radic Biol Med 36, 1155-1162
    • (2004) Free Radic Biol Med , vol.36 , pp. 1155-1162
    • Choi, J.1    Forster, M.J.2    McDonald, S.R.3    Weintraub, S.T.4    Carroll, C.A.5    Gracy, R.W.6
  • 53
    • 15744398884 scopus 로고    scopus 로고
    • Oxidative modifications and aggregation of Cu, Zn-Superoxide dismutase associated with Alzheimer and Parkinson diseases
    • Choi J, Rees HD, Weintraub ST, Levey AI, Chin LS, Li L (2005) Oxidative modifications and aggregation of Cu, Zn-Superoxide dismutase associated with Alzheimer and Parkinson diseases. J Biol Chem 280, 11648-11655
    • (2005) J Biol Chem , vol.280 , 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
  • 54
    • 71549148116 scopus 로고    scopus 로고
    • Mitochondrial ATP-Synthase in the entorhinal cortex is a target of oxidative stress at stages i/ii of alzheimer's disease pathology
    • Terni B, Boada J, Portero-Otin M, Pamplona R, Ferrer I (2010) Mitochondrial ATP-Synthase in the Entorhinal Cortex Is a Target of Oxidative Stress at Stages I/II of Alzheimer's Disease Pathology. Brain Pathol 20, 222-233
    • (2010) Brain Pathol , vol.20 , pp. 222-233
    • Terni, B.1    Boada, J.2    Portero-Otin, M.3    Pamplona, R.4    Ferrer, I.5
  • 55
    • 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 DA, Poon HF, St Clair D, Keller JN, Pierce WM, Klein JB, Markesbery WR (2006) Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease. Neurobiol Dis 22, 223-232
    • (2006) Neurobiol Dis , vol.22 , 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
  • 56
    • 67349253085 scopus 로고    scopus 로고
    • Oxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: Role of Abeta in pathogenesis
    • Sultana R, Perluigi M, Butterfield DA (2009) Oxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: Role of Abeta in pathogenesis. Acta Neuropathol 118, 131-150
    • (2009) Acta Neuropathol , vol.118 , pp. 131-150
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 59
    • 34247142905 scopus 로고    scopus 로고
    • Elevated levels of 3-Nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: Implications for the role of nitration in the progression of Alzheimer's disease
    • Butterfield DA, Reed TT, Perluigi M, De Marco C, Coccia R, Keller JN, Markesbery WR, Sultana R (2007) Elevated levels of 3-Nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: Implications for the role of nitration in the progression of Alzheimer's disease. Brain Res 1148, 243-248
    • (2007) Brain Res , vol.1148 , pp. 243-248
    • Butterfield, D.A.1    Reed, T.T.2    Perluigi, M.3    De Marco, C.4    Coccia, R.5    Keller, J.N.6    Markesbery, W.R.7    Sultana, R.8
  • 60
    • 45049086702 scopus 로고    scopus 로고
    • Effects of oxidative and nitrosative stress in brain on p53 proapoptotic protein in amnestic mild cognitive impairment and Alzheimer disease
    • Cenini G, Sultana R, Memo M, Butterfield DA (2008) Effects of oxidative and nitrosative stress in brain on p53 proapoptotic protein in amnestic mild cognitive impairment and Alzheimer disease. Free Radic Biol Med 45, 81-85
    • (2008) Free Radic Biol Med , vol.45 , pp. 81-85
    • Cenini, G.1    Sultana, R.2    Memo, M.3    Butterfield, D.A.4
  • 63
    • 64249133725 scopus 로고    scopus 로고
    • S-Nitrosylation of Drp1 mediates betaamyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, Cieplak P, Godzik A, Gu Z, Lipton SA (2009) S-Nitrosylation of Drp1 mediates betaamyloid-related mitochondrial fission and neuronal injury. Science 324, 102-105
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 64
    • 75949083202 scopus 로고    scopus 로고
    • Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates
    • Martinez A, Portero-Otin M, Pamplona R, Ferrer I (2009) Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol 20, 281-297
    • (2009) Brain Pathol , vol.20 , pp. 281-297
    • Martinez, A.1    Portero-Otin, M.2    Pamplona, R.3    Ferrer, I.4
  • 65
    • 70350129134 scopus 로고    scopus 로고
    • Multifunctional roles of enolase in Alzheimer's disease brain: Beyond altered glucose metabolism
    • Butterfield DA, Lange ML (2009) Multifunctional roles of enolase in Alzheimer's disease brain: Beyond altered glucose metabolism. J Neurochem 111, 915-933
    • (2009) J Neurochem , vol.111 , pp. 915-933
    • Butterfield, D.A.1    Lange, M.L.2
  • 66
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L, Roeder RG, Luo Y (2003) S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114, 255-266
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 67
    • 46449101370 scopus 로고    scopus 로고
    • Role of glyceraldehyde-3-Phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum
    • Bryksin AV, Laktionov PP (2008) Role of glyceraldehyde-3-Phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum. Biochemistry (Mosc) 73, 619-625
    • (2008) Biochemistry (Mosc , vol.73 , pp. 619-625
    • Bryksin, A.V.1    Laktionov, P.P.2
  • 68
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: A novel cell death cascade
    • Hara MR, Snyder SH (2006) Nitric oxide-GAPDH-Siah: A novel cell death cascade. Cell Mol Neurobiol 26, 527-538
    • (2006) Cell Mol Neurobiol , vol.26 , pp. 527-538
    • Hara, M.R.1    Snyder, S.H.2
  • 69
    • 0030887909 scopus 로고    scopus 로고
    • Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-Phosphate dehydrogenase
    • Puder M, Soberman RJ (1997) Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-Phosphate dehydrogenase. J Biol Chem 272, 10936-10940
    • (1997) J Biol Chem , vol.272 , pp. 10936-10940
    • Puder, M.1    Soberman, R.J.2
  • 70
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-Phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-Amyloid precursor protein
    • Schulze H, Schuler A, Stuber D, Dobeli H, Langen H, Huber G (1993) Rat brain glyceraldehyde-3-Phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-Amyloid precursor protein. J Neurochem 60, 1915-1922
    • (1993) J Neurochem , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 73
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-Associated phosphorylated tau protein
    • Lu PJ,Wulf G, Zhou XZ, Davies P, Lu KP (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-Associated phosphorylated tau protein. Nature 399, 784-788
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 74
    • 75149118997 scopus 로고    scopus 로고
    • Role of oxidative stress in the progression of Alzheimer's disease
    • Sultana R, Butterfield DA (2010) Role of oxidative stress in the progression of Alzheimer's disease. J Alzheimers Dis 19, 341-353
    • (2010) J Alzheimers Dis , vol.19 , pp. 341-353
    • Sultana, R.1    Butterfield, D.A.2
  • 75
    • 70350089195 scopus 로고    scopus 로고
    • Redox proteomics identification of HNE-Modified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis
    • Perluigi M, Sultana R, Cenini G, Di Domenico F, Memo M, Pierce WM, Coccia R, Butterfield DA (2009) Redox proteomics identification of HNE-Modified brain proteins in Alzheimer's disease: Role of lipid peroxidation in Alzheimer's disease pathogenesis. Proteomics Clin Appl 13, 682-693
    • (2009) Proteomics Clin Appl , vol.13 , pp. 682-693
    • Perluigi, M.1    Sultana, R.2    Cenini, G.3    Di Domenico, F.4    Memo, M.5    Pierce, W.M.6    Coccia, R.7    Butterfield, D.A.8
  • 76
    • 39249083317 scopus 로고    scopus 로고
    • Loss of phospholipid asymmetry and elevated brain apoptotic protein levels in subjects with amnestic mild cognitive impairment and Alzheimer disease
    • Bader Lange ML, Cenini G, Piroddi M, Abdul HM, Sultana R, Galli F,MemoM, ButterfieldDA(2008) Loss of phospholipid asymmetry and elevated brain apoptotic protein levels in subjects with amnestic mild cognitive impairment and Alzheimer disease. Neurobiol Dis 29, 456-464
    • (2008) Neurobiol Dis , vol.29 , pp. 456-464
    • Bader Lange, M.L.1    Cenini, G.2    Piroddi, M.3    Abdul, H.M.4    Sultana, R.5    Galli, F.6    Memo, M.7    Butterfield, D.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.