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Volumn 27, Issue 1, 2006, Pages 42-53

Oxidative modification of proteins in the frontal cortex of Alzheimer's disease brain

Author keywords

Alzheimer's disease; Frontal cortex; Human brain; Mass spectrometry; Neuropathology; Oxidative stress; Protein carbonyls; Protein oxidation; Proteomics; Two dimensional gel electrophoresis

Indexed keywords

BRAIN PROTEIN; GLUTAMATE DEHYDROGENASE; MALATE DEHYDROGENASE; MITOCHONDRIAL ENZYME;

EID: 27744576098     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2004.11.010     Document Type: Article
Times cited : (93)

References (65)
  • 1
    • 0034024347 scopus 로고    scopus 로고
    • Oxidative modification of creatine kinase BB in Alzheimer's disease brain
    • M. Aksenov, M. Aksenova, D.A. Butterfield, and W.R. Markesbery Oxidative modification of creatine kinase BB in Alzheimer's disease brain J Neurochem 74 6 2000 2520 2527
    • (2000) J Neurochem , vol.74 , Issue.6 , pp. 2520-2527
    • Aksenov, M.1    Aksenova, M.2    Butterfield, D.A.3    Markesbery, W.R.4
  • 3
    • 0032966889 scopus 로고    scopus 로고
    • Beta-amyloid load is not influenced by the severity of cardiovascular disease in aged and demented patients
    • I. Alafuzoff, S. Helisalmi, A. Mannermaa, P. Riekkinen Sr., and H. Soininen Beta-amyloid load is not influenced by the severity of cardiovascular disease in aged and demented patients Stroke 30 3 1999 613 618
    • (1999) Stroke , vol.30 , Issue.3 , pp. 613-618
    • Alafuzoff, I.1    Helisalmi, S.2    Mannermaa, A.3    Riekkinen Sr., P.4    Soininen, H.5
  • 5
    • 0141853765 scopus 로고    scopus 로고
    • Amyloid-beta: A chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-beta
    • C.S. Atwood, M.E. Obrenovich, T. Liu, H. Chan, G. Perry, and M.A. Smith Amyloid-beta: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-beta Brain Res Brain Res Rev 43 1 2003 1 16
    • (2003) Brain Res Brain Res Rev , vol.43 , Issue.1 , pp. 1-16
    • Atwood, C.S.1    Obrenovich, M.E.2    Liu, T.3    Chan, H.4    Perry, G.5    Smith, M.A.6
  • 6
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • B.S. Berlett, and E.R. Stadtman Protein oxidation in aging, disease, and oxidative stress J Biol Chem 272 33 1997 20313 20316
    • (1997) J Biol Chem , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 7
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • A.C. Bowling, and M.F. Beal Bioenergetic and oxidative stress in neurodegenerative diseases Life Sci 56 14 1995 1151 1171
    • (1995) Life Sci , vol.56 , Issue.14 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 8
    • 0026134421 scopus 로고
    • Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
    • H. Braak, and E. Braak Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections Brain Pathol 1 3 1991 213 216
    • (1991) Brain Pathol , vol.1 , Issue.3 , pp. 213-216
    • Braak, H.1    Braak, E.2
  • 9
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological stageing of Alzheimer-related changes Acta Neuropathol (Berl) 82 4 1991 239 259
    • (1991) Acta Neuropathol (Berl) , vol.82 , Issue.4 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 10
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • D.A. Butterfield, and J. Kanski Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins Mech Ageing Dev 122 9 2001 945 962
    • (2001) Mech Ageing Dev , vol.122 , Issue.9 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 11
    • 0025650037 scopus 로고
    • Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease
    • R.F. Butterworth, and A.M. Besnard Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease Metab Brain Dis 5 4 1990 179 184
    • (1990) Metab Brain Dis , vol.5 , Issue.4 , pp. 179-184
    • Butterworth, R.F.1    Besnard, A.M.2
  • 12
    • 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
    • A. Castegna, M. Aksenov, M. Aksenova, V. Thongboonkerd, J. Klein, and W. Pierce 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 4 2002 62
    • (2002) Free Radic Biol Med , vol.33 , Issue.4 , pp. 62
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.5    Pierce, W.6
  • 13
    • 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
    • A. Castegna, M. Aksenov, V. Thongboonkerd, J.B. Klein, W.M. Pierce, and R. Booze Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71 J Neurochem 82 6 2002 524 532
    • (2002) J Neurochem , vol.82 , Issue.6 , pp. 524-532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6
  • 14
    • 0023879595 scopus 로고
    • Influence of the malate-aspartate shuttle on oxidative metabolism in synaptosomes
    • A.J. Cheeseman, and J.B. Clark Influence of the malate-aspartate shuttle on oxidative metabolism in synaptosomes J Neurochem 50 5 1988 1559 1565
    • (1988) J Neurochem , vol.50 , Issue.5 , pp. 1559-1565
    • Cheeseman, A.J.1    Clark, J.B.2
  • 15
    • 0038823734 scopus 로고    scopus 로고
    • Proteomic comparison between human young and old brains by two-dimensional gel electrophoresis and identification of proteins
    • W. Chen, J. Ji, X. Xu, S. He, and B. Ru Proteomic comparison between human young and old brains by two-dimensional gel electrophoresis and identification of proteins Int J Dev Neurosci 21 4 2003 209 216
    • (2003) Int J Dev Neurosci , vol.21 , Issue.4 , pp. 209-216
    • Chen, W.1    Ji, J.2    Xu, X.3    He, S.4    Ru, B.5
  • 16
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: Protein carbonyl content as a marker of damage
    • M. Chevion, E. Berenshtein, and E.R. Stadtman Human studies related to protein oxidation: protein carbonyl content as a marker of damage Free Radic Res 33 Suppl. 2000 S99 S108
    • (2000) Free Radic Res , vol.33 , Issue.SUPPL.
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 19
    • 0023809230 scopus 로고
    • Alzheimer's disease. a double-labeling immunohistochemical study of senile plaques
    • D.W. Dickson, J. Farlo, P. Davies, H. Crystal, P. Fuld, and S.H. Yen Alzheimer's disease. A double-labeling immunohistochemical study of senile plaques Am J Pathol 132 1 1988 86 101
    • (1988) Am J Pathol , vol.132 , Issue.1 , pp. 86-101
    • Dickson, D.W.1    Farlo, J.2    Davies, P.3    Crystal, H.4    Fuld, P.5    Yen, S.H.6
  • 20
    • 0025326250 scopus 로고
    • Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes
    • M. Erecinska, and D. Nelson Activation of glutamate dehydrogenase by leucine and its nonmetabolizable analogue in rat brain synaptosomes J Neurochem 54 4 1990 1335 1343
    • (1990) J Neurochem , vol.54 , Issue.4 , pp. 1335-1343
    • Erecinska, M.1    Nelson, D.2
  • 21
    • 0023730342 scopus 로고
    • Glucose and synaptosomal glutamate metabolism: Studies with [15N] glutamate
    • M. Erecinska, M.M. Zaleska, I. Nissim, D. Nelson, F. Dagani, and M. Yudkoff Glucose and synaptosomal glutamate metabolism: studies with [15N] glutamate J Neurochem 51 3 1988 892 902
    • (1988) J Neurochem , vol.51 , Issue.3 , pp. 892-902
    • Erecinska, M.1    Zaleska, M.M.2    Nissim, I.3    Nelson, D.4    Dagani, F.5    Yudkoff, M.6
  • 22
    • 0024317904 scopus 로고
    • Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported
    • D.A. Evans, H.H. Funkenstein, M.S. Albert, P.A. Scherr, N.R. Cook, and M.J. Chown Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported JAMA 262 18 1989 2551 2556
    • (1989) JAMA , vol.262 , Issue.18 , pp. 2551-2556
    • Evans, D.A.1    Funkenstein, H.H.2    Albert, M.S.3    Scherr, P.A.4    Cook, N.R.5    Chown, M.J.6
  • 23
    • 0035151481 scopus 로고    scopus 로고
    • Postmortem changes in the level of brain proteins
    • M. Fountoulakis, R. Hardmeier, H. Höger, and G. Lubec Postmortem changes in the level of brain proteins Exp Neurol 167 1 2001 86 94
    • (2001) Exp Neurol , vol.167 , Issue.1 , pp. 86-94
    • Fountoulakis, M.1    Hardmeier, R.2    Höger, H.3    Lubec, G.4
  • 24
    • 0142244521 scopus 로고    scopus 로고
    • Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome
    • B. Franzén, Y. Yang, D. Sunnemark, M. Wickman, J. Ottervald, and M. Oppermann Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome Proteomics 3 10 2003 1920 1929
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1920-1929
    • Franzén, B.1    Yang, Y.2    Sunnemark, D.3    Wickman, M.4    Ottervald, J.5    Oppermann, M.6
  • 25
    • 0033382224 scopus 로고    scopus 로고
    • Oxidative stress and a key metabolic enzyme in Alzheimer brains, cultured cells, and an animal model of chronic oxidative deficits
    • G.E. Gibson, L.C. Park, H. Zhang, S. Sorbi, and N.Y. Calingasan Oxidative stress and a key metabolic enzyme in Alzheimer brains, cultured cells, and an animal model of chronic oxidative deficits Ann NY Acad Sci 893 1999 79 94
    • (1999) Ann NY Acad Sci , vol.893 , pp. 79-94
    • Gibson, G.E.1    Park, L.C.2    Zhang, H.3    Sorbi, S.4    Calingasan, N.Y.5
  • 26
    • 0025257612 scopus 로고
    • Restriction isotyping of human apolipoprotein e by gene amplification and cleavage with HhaI determination by PCR-RFLP of apo e genotype in a Japanese population
    • J.E. Hixson, D.T. Vernier, K. Tsukamoto, T. Watanabe, T. Matsushima, and M. Kinoshita Restriction isotyping of human apolipoprotein E by gene amplification and cleavage with HhaI determination by PCR-RFLP of apo E genotype in a Japanese population J Lipid Res 31 3 1990 545 548
    • (1990) J Lipid Res , vol.31 , Issue.3 , pp. 545-548
    • Hixson, J.E.1    Vernier, D.T.2    Tsukamoto, K.3    Watanabe, T.4    Matsushima, T.5    Kinoshita, M.6
  • 27
    • 0037998074 scopus 로고    scopus 로고
    • Biochemical and molecular studies using human autopsy brain tissue
    • M.W. Hynd, J.M. Lewohl, H.L. Scott, and P.R. Dodd Biochemical and molecular studies using human autopsy brain tissue J Neurochem 85 3 2003 543 562
    • (2003) J Neurochem , vol.85 , Issue.3 , pp. 543-562
    • Hynd, M.W.1    Lewohl, J.M.2    Scott, H.L.3    Dodd, P.R.4
  • 28
    • 0023645832 scopus 로고
    • Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase
    • T. Joh, H. Takeshima, T. Tsuzuki, C. Setoyama, K. Shimada, and S. Tanase Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase J Biol Chem 262 31 1987 15127 15131
    • (1987) J Biol Chem , vol.262 , Issue.31 , pp. 15127-15131
    • Joh, T.1    Takeshima, H.2    Tsuzuki, T.3    Setoyama, C.4    Shimada, K.5    Tanase, S.6
  • 29
    • 0032401643 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress are significantly elevated in Down syndrome
    • S.V. Jovanovic, D. Clements, and K. MacLeod Biomarkers of oxidative stress are significantly elevated in Down syndrome Free Radic Biol Med 25 9 1998 1044 1048
    • (1998) Free Radic Biol Med , vol.25 , Issue.9 , pp. 1044-1048
    • Jovanovic, S.V.1    Clements, D.2    MacLeod, K.3
  • 30
    • 0036080348 scopus 로고    scopus 로고
    • Aspartate aminotransferase isotope exchange reactions: Implications for glutamate/glutamine shuttle hypothesis
    • G.A. Kimmich, J.A. Roussie, and J. Randles Aspartate aminotransferase isotope exchange reactions: implications for glutamate/glutamine shuttle hypothesis Am J Physiol Cell Physiol 282 6 2002 C1404 C1413
    • (2002) Am J Physiol Cell Physiol , vol.282 , Issue.6
    • Kimmich, G.A.1    Roussie, J.A.2    Randles, J.3
  • 32
    • 0344406145 scopus 로고    scopus 로고
    • Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders
    • K. Krapfenbauer, E. Engidawork, N. Cairns, M. Fountoulakis, and G. Lubec Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders Brain Res 967 1-2 2003 152 160
    • (2003) Brain Res , vol.967 , Issue.1-2 , pp. 152-160
    • Krapfenbauer, K.1    Engidawork, E.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 33
    • 0031780444 scopus 로고    scopus 로고
    • Pitfalls in the quantitative estimation of beta-amyloid immunoreactivity in human brain tissue
    • M. Kraszpulski, H. Soininen, P. Riekkinen Sr., and I. Alafuzoff Pitfalls in the quantitative estimation of beta-amyloid immunoreactivity in human brain tissue Histochem Cell Biol 110 4 1998 439 445
    • (1998) Histochem Cell Biol , vol.110 , Issue.4 , pp. 439-445
    • Kraszpulski, M.1    Soininen, H.2    Riekkinen Sr., P.3    Alafuzoff, I.4
  • 34
    • 0030920364 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometric peptide mapping of the neural cell adhesion protein neurolin purified by sodium dodecyl sulfate polyacrylamide gel electrophoresis or acidic precipitation
    • M. Kussmann, U. Lassing, C.A. Sturmer, M. Przybylski, and P. Roepstorff Matrix-assisted laser desorption/ionization mass spectrometric peptide mapping of the neural cell adhesion protein neurolin purified by sodium dodecyl sulfate polyacrylamide gel electrophoresis or acidic precipitation J Mass Spectrom 32 5 1997 483 493
    • (1997) J Mass Spectrom , vol.32 , Issue.5 , pp. 483-493
    • Kussmann, M.1    Lassing, U.2    Sturmer, C.A.3    Przybylski, M.4    Roepstorff, P.5
  • 35
    • 0344305371 scopus 로고    scopus 로고
    • Morphogenesis of Lewy bodies: Dissimilar incorporation of alpha-synuclein, ubiquitin, and p62
    • E. Kuusisto, L. Parkkinen, and I. Alafuzoff Morphogenesis of Lewy bodies: dissimilar incorporation of alpha-synuclein, ubiquitin, and p62 J Neuropathol Exp Neurol 62 12 2003 1241 1253
    • (2003) J Neuropathol Exp Neurol , vol.62 , Issue.12 , pp. 1241-1253
    • Kuusisto, E.1    Parkkinen, L.2    Alafuzoff, I.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 259 1970 680 685
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • R.L. Levine, J.A. Williams, E.R. Stadtman, and E. Shacter Carbonyl assays for determination of oxidatively modified proteins Meth Enzymol 233 1994 346 357
    • (1994) Meth Enzymol , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 38
    • 0027412177 scopus 로고
    • Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain
    • P. Malik, M.C. McKenna, and J.T. Tildon Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain Neurochem Res 18 3 1993 247 257
    • (1993) Neurochem Res , vol.18 , Issue.3 , pp. 247-257
    • Malik, P.1    McKenna, M.C.2    Tildon, J.T.3
  • 39
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • M. Mann, and O.N. Jensen Proteomic analysis of post-translational modifications Nat Biotechnol 21 3 2003 255 261
    • (2003) Nat Biotechnol , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 40
    • 0034256931 scopus 로고    scopus 로고
    • Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals
    • M.C. McKenna, J.H. Stevenson, X. Huang, and I.B. Hopkins Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals Neurochem Int 37 2-3 2000 229 241
    • (2000) Neurochem Int , vol.37 , Issue.2-3 , pp. 229-241
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Hopkins, I.B.4
  • 41
    • 0033982623 scopus 로고    scopus 로고
    • Mitochondrial malic enzyme activity is much higher in mitochondria from cortical synaptic terminals compared with mitochondria from primary cultures of cortical neurons or cerebellar granule cells
    • M.C. McKenna, J.H. Stevenson, X. Huang, J.T. Tildon, C.L. Zielke, and I.B. Hopkins Mitochondrial malic enzyme activity is much higher in mitochondria from cortical synaptic terminals compared with mitochondria from primary cultures of cortical neurons or cerebellar granule cells Neurochem Int 36 4-5 2000 451 459
    • (2000) Neurochem Int , vol.36 , Issue.4-5 , pp. 451-459
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Tildon, J.T.4    Zielke, C.L.5    Hopkins, I.B.6
  • 42
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • G. McKhann, D. Drachman, M. Folstein, R. Katzman, D. Price, and E.M. Stadlan Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease Neurology 34 7 1984 939 944
    • (1984) Neurology , vol.34 , Issue.7 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 43
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • S.S. Mirra, A. Heyman, D. McKeel, SM. Sumi, B.J. Crain, and L.M. Brownlee The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease Neurology 41 4 1991 479 486
    • (1991) Neurology , vol.41 , Issue.4 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 44
    • 0027225463 scopus 로고
    • Plasma concentrations of glutamate and its metabolites in patients with Alzheimer's disease
    • D.E. Miulli, D.Y. Norwell, and F.N. Schwartz Plasma concentrations of glutamate and its metabolites in patients with Alzheimer's disease J Am Osteopath Assoc 93 6 1993 670 676
    • (1993) J Am Osteopath Assoc , vol.93 , Issue.6 , pp. 670-676
    • Miulli, D.E.1    Norwell, D.Y.2    Schwartz, F.N.3
  • 45
    • 0032698449 scopus 로고    scopus 로고
    • Newer aspects of glutamine/glutamate metabolism: The role of acute pH changes
    • I. Nissim Newer aspects of glutamine/glutamate metabolism: the role of acute pH changes Am J Physiol 277 3 1999 F493 F497
    • (1999) Am J Physiol , vol.277 , Issue.3
    • Nissim, I.1
  • 46
    • 0033946833 scopus 로고    scopus 로고
    • Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes
    • T.A. Nyman, S. Matikainen, T. Sareneva, I. Julkunen, and N. Kalkkinen Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes Eur J Biochem 267 13 2000 4011 4019
    • (2000) Eur J Biochem , vol.267 , Issue.13 , pp. 4011-4019
    • Nyman, T.A.1    Matikainen, S.2    Sareneva, T.3    Julkunen, I.4    Kalkkinen, N.5
  • 48
    • 0017295228 scopus 로고
    • Some cerebral proteins and enzyme systems in Alzheimer's presenile and senile dementia
    • W. Op den Velde, and F.C. Stam Some cerebral proteins and enzyme systems in Alzheimer's presenile and senile dementia J Am Geriatr Soc 24 1 1976 12 16
    • (1976) J Am Geriatr Soc , vol.24 , Issue.1 , pp. 12-16
    • Op Den Velde, W.1    Stam, F.C.2
  • 53
    • 0037085011 scopus 로고    scopus 로고
    • Alzheimer's disease and oxygen radicals: New insights
    • D. Pratico Alzheimer's disease and oxygen radicals: new insights Biochem Pharmacol 63 4 2002 563 567
    • (2002) Biochem Pharmacol , vol.63 , Issue.4 , pp. 563-567
    • Pratico, D.1
  • 54
    • 0342327317 scopus 로고    scopus 로고
    • Diagnosis of Alzheimer's disease with cerebrospinal fluid tau protein and aspartate aminotransferase
    • M. Riemenschneider, K. Buch, M. Schmolke, A. Kurz, and W.G. Guder Diagnosis of Alzheimer's disease with cerebrospinal fluid tau protein and aspartate aminotransferase Lancet 350 9080 1997 784
    • (1997) Lancet , vol.350 , Issue.9080 , pp. 784
    • Riemenschneider, M.1    Buch, K.2    Schmolke, M.3    Kurz, A.4    Guder, W.G.5
  • 55
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • J. Rosenfeld, J. Capdevielle, J.C. Guillemot, and P. Ferrara In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis Anal Biochem 203 1 1992 173 179
    • (1992) Anal Biochem , vol.203 , Issue.1 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 56
    • 0021813419 scopus 로고
    • An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain
    • K.F. Sheu, Y.T. Kim, J.P. Blass, and M.E. Weksler An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain Ann Neurol 17 5 1985 444 449
    • (1985) Ann Neurol , vol.17 , Issue.5 , pp. 444-449
    • Sheu, K.F.1    Kim, Y.T.2    Blass, J.P.3    Weksler, M.E.4
  • 57
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal Chem 68 5 1996 850 858
    • (1996) Anal Chem , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 58
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • R. Shringarpure, and K.J. Davies Protein turnover by the proteasome in aging and disease Free Radic Biol Med 32 11 2000 1084 1089
    • (2000) Free Radic Biol Med , vol.32 , Issue.11 , pp. 1084-1089
    • Shringarpure, R.1    Davies, K.J.2
  • 59
    • 0032438035 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts
    • N. Sitte, K. Merker, and T. Grune Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts FEBS Lett 440 3 1998 399 402
    • (1998) FEBS Lett , vol.440 , Issue.3 , pp. 399-402
    • Sitte, N.1    Merker, K.2    Grune, T.3
  • 60
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4- dinitrophenylhydrazine
    • M.A. Smith, L.M. Sayre, V.E. Anderson, P.L. Harris, M.F. Beal, and N. Kowall Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4- dinitrophenylhydrazine J Histochem Cytochem 46 6 1998 731 735
    • (1998) J Histochem Cytochem , vol.46 , Issue.6 , pp. 731-735
    • Smith, M.A.1    Sayre, L.M.2    Anderson, V.E.3    Harris, P.L.4    Beal, M.F.5    Kowall, N.6
  • 61
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • E.R. Stadtman, and R.L. Levine Free radical-mediated oxidation of free amino acids and amino acid residues in proteins Amino Acids 25 3-4 2003 207 218
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 62
    • 0032566190 scopus 로고    scopus 로고
    • Increased aspartate aminotransferase activity in cerebrospinal fluid and Alzheimer's disease
    • T. Tapiola, M. Lehtovirta, T. Pirttilä, I. Alafuzoff, P. Riekkinen, and H. Soininen Increased aspartate aminotransferase activity in cerebrospinal fluid and Alzheimer's disease Lancet 352 9124 1998 287
    • (1998) Lancet , vol.352 , Issue.9124 , pp. 287
    • Tapiola, T.1    Lehtovirta, M.2    Pirttilä, T.3    Alafuzoff, I.4    Riekkinen, P.5    Soininen, H.6
  • 63
    • 0036807924 scopus 로고    scopus 로고
    • Proteomic profiling and neurodegeneration in Alzheimer's disease
    • T. Tsuji, A. Shiozaki, R. Kohno, K. Yoshizato, and S. Shimohama Proteomic profiling and neurodegeneration in Alzheimer's disease Neurochem Res 27 10 2002 1245 1253
    • (2002) Neurochem Res , vol.27 , Issue.10 , pp. 1245-1253
    • Tsuji, T.1    Shiozaki, A.2    Kohno, R.3    Yoshizato, K.4    Shimohama, S.5
  • 65
    • 0028036798 scopus 로고
    • Tricarboxylic acid cycle in rat brain synaptosomes. Fluxes and interactions with aspartate aminotransferase and malate/aspartate shuttle
    • M. Yudkoff, D. Nelson, Y. Daikhin, and M. Erecinska Tricarboxylic acid cycle in rat brain synaptosomes. Fluxes and interactions with aspartate aminotransferase and malate/aspartate shuttle J Biol Chem 269 44 1994 27414 27420
    • (1994) J Biol Chem , vol.269 , Issue.44 , pp. 27414-27420
    • Yudkoff, M.1    Nelson, D.2    Daikhin, Y.3    Erecinska, M.4


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