메뉴 건너뛰기




Volumn 65, Issue , 2013, Pages 595-606

Lymphocyte mitochondria: Toward identification of peripheral biomarkers in the progression of Alzheimer disease

Author keywords

Alzheimer disease; Free radicals; Lymphocytes; Mild cognitive impairment; Mitochondria; Oxidative stress; Peripheral biomarker; Proteomics

Indexed keywords

ALPHA TOCOPHEROL; BETA CAROTENE; BIOLOGICAL MARKER; MYOSIN LIGHT CHAIN; MYOSIN LIGHT POLYPEPTIDE 6; PEROXIREDOXIN 3; POLYPEPTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE BETA; UNCLASSIFIED DRUG;

EID: 84884528242     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.08.001     Document Type: Article
Times cited : (56)

References (66)
  • 2
    • 0042023711 scopus 로고    scopus 로고
    • Alzheimer disease in the US population: Prevalence estimates using the 2000 census
    • DOI 10.1001/archneur.60.8.1119
    • L.E. Hebert, P.A. Scherr, J.L. Bienias, D.A. Bennett, and D.A. Evans Alzheimer disease in the US population: prevalence estimates using the 2000 census Arch. Neurol. 60 2003 1119 1122 (Pubitemid 36975801)
    • (2003) Archives of Neurology , vol.60 , Issue.8 , pp. 1119-1122
    • Hebert, L.E.1    Scherr, P.A.2    Bienias, J.L.3    Bennett, D.A.4    Evans, D.A.5
  • 3
    • 0342980328 scopus 로고    scopus 로고
    • In vivo PET imaging and postmortem studies suggest potentially reversible and irreversible stages of brain metabolic failure in Alzheimer's disease
    • S.I. Rapoport In vivo PET imaging and postmortem studies suggest potentially reversible and irreversible stages of brain metabolic failure in Alzheimer's disease Eur. Arch. Psychiatry Clin. Neurosci 249 Suppl. 3 1999 46 55
    • (1999) Eur. Arch. Psychiatry Clin. Neurosci , vol.249 , Issue.SUPPL. 3 , pp. 46-55
    • Rapoport, S.I.1
  • 4
    • 0035928402 scopus 로고    scopus 로고
    • Imaging of onset and progression of Alzheimer's disease with voxel-compression mapping of serial magnetic resonance images
    • DOI 10.1016/S0140-6736(01)05408-3
    • N.C. Fox, W.R. Crum, R.I. Scahill, J.M. Stevens, J.C. Janssen, and M.N. Rossor Imaging of onset and progression of Alzheimer's disease with voxel-compression mapping of serial magnetic resonance images Lancet 358 2001 201 205 (Pubitemid 32718544)
    • (2001) Lancet , vol.358 , Issue.9277 , pp. 201-205
    • Fox, N.C.1    Crum, W.R.2    Scahill, R.I.3    Stevens, J.M.4    Janssen, J.C.5    Rossor, M.N.6
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • D.J. Selkoe Alzheimer's disease: genes, proteins, and therapy Physiol. Rev. 81 2001 741 766 (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 6
    • 10844269704 scopus 로고    scopus 로고
    • Role of phenylalanine 20 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • DOI 10.1021/tx049796w
    • D. Boyd-Kimball, H. Mohmmad Abdul, T. Reed, R. Sultana, and D.A. Butterfield Role of phenylalanine 20 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity Chem. Res. Toxicol. 17 2004 1743 1749 (Pubitemid 39665568)
    • (2004) Chemical Research in Toxicology , vol.17 , Issue.12 , pp. 1743-1749
    • Boyd-Kimball, D.1    Abdul, H.M.2    Reed, T.3    Sultana, R.4    Butterfield, D.A.5
  • 7
    • 15744387176 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid β-peptide (1-42) into rat brain: Implications for Alzheimer's disease
    • DOI 10.1016/j.neuroscience.2004.12.022
    • D. Boyd-Kimball, R. Sultana, H.F. Poon, B.C. Lynn, F. Casamenti, G. Pepeu, J.B. Klein, and D.A. Butterfield 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 2005 313 324 (Pubitemid 40417906)
    • (2005) Neuroscience , vol.132 , Issue.2 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Fai Poon, H.3    Lynn, B.C.4    Casamenti, F.5    Pepeu, G.6    Klein, J.B.7    Butterfield, D.A.8
  • 8
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • DOI 10.1016/j.bbapap.2004.10.014, PII S1570963904002961, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • D.A. Butterfield, and D. Boyd-Kimball The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity Biochim. Biophys. Acta 1703 2005 149 156 (Pubitemid 40170438)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 10
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • DOI 10.1016/S0891-5849(96)00629-6, PII S0891584996006296
    • W.R. Markesbery Oxidative stress hypothesis in Alzheimer's disease Free Radic. Biol. Med. 23 1997 134 147 (Pubitemid 27217017)
    • (1997) Free Radical Biology and Medicine , vol.23 , Issue.1 , pp. 134-147
    • Markesbery, W.R.1
  • 12
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • DOI 10.1016/S0197-4580(98)00009-8, PII S0197458098000098
    • W.R. Markesbery, and M.A. Lovell 4-Hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease Neurobiol. Aging 19 1998 33 36 (Pubitemid 28167792)
    • (1998) Neurobiology of Aging , vol.19 , Issue.1 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 14
    • 0031028437 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4
    • K.S. Montine, S.J. Olson, V. Amarnath, W.O. Whetsell Jr, D.G. Graham, and T.J. Montine Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4 Am. J. Pathol. 150 1997 437 443 (Pubitemid 27073773)
    • (1997) American Journal of Pathology , vol.150 , Issue.2 , pp. 437-443
    • Montine, K.S.1    Oison, S.J.2    Amarnath, V.3    Whetsell Jr., W.O.4    Graham, D.G.5    Montine, T.J.6
  • 15
    • 2342420034 scopus 로고    scopus 로고
    • Lipid Peroxidation and Oxidative imbalance: Early functional events in Alzheimer's disease
    • D. Pratico, and S. Sung Lipid peroxidation and oxidative imbalance: early functional events in Alzheimer's disease J. Alzheimers Dis. 6 2004 171 175 (Pubitemid 38560253)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.2 , pp. 171-175
    • Pratico, D.1    Sung, S.2
  • 17
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • K. Hensley, M.L. Maidt, Z. Yu, H. Sang, W.R. Markesbery, and R.A. Floyd Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation J. Neurosci. 18 1998 8126 8132 (Pubitemid 28464991)
    • (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
  • 18
    • 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 Aβ1-42
    • DOI 10.1046/j.1471-4159.2001.00451.x
    • C.M. Lauderback, J.M. Hackett, F.F. Huang, J.N. Keller, L.I. Szweda, W.R. Markesbery, and 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 Abeta1-42 J. Neurochem. 78 2001 413 416 (Pubitemid 32664423)
    • (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    Allan Butterfield, D.7
  • 21
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • DOI 10.1096/fj.05-3735fje
    • C. Caspersen, N. Wang, J. Yao, A. Sosunov, X. Chen, J.W. Lustbader, H.W. Xu, D. Stern, G. McKhann, and S.D. Yan Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease FASEB J 19 2005 2040 2041 (Pubitemid 41759758)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3    Sosunov, A.4    Chen, X.5    Lustbader, J.W.6    Xu, H.W.7    Stern, D.8    McKhann, G.9    Yan, S.D.10
  • 22
    • 67649803186 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease
    • P.H. Reddy Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease Exp. Neurol. 218 2009 286 292
    • (2009) Exp. Neurol. , vol.218 , pp. 286-292
    • Reddy, P.H.1
  • 23
    • 70449411818 scopus 로고    scopus 로고
    • Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment
    • R. Sultana, and D.A. Butterfield Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment J. Bioenerg. Biomembr. 41 2009 441 446
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 441-446
    • Sultana, R.1    Butterfield, D.A.2
  • 24
    • 77956219269 scopus 로고    scopus 로고
    • Rethinking Alzheimer's disease therapy: Are mitochondria the key?
    • M. Ankarcrona, F. Mangialasche, and B. Winblad Rethinking Alzheimer's disease therapy: are mitochondria the key? J. Alzheimers Dis. 20 Suppl. 2 2010 S579 590
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.SUPPL. 2 , pp. 579-590
    • Ankarcrona, M.1    Mangialasche, F.2    Winblad, B.3
  • 25
    • 79955658979 scopus 로고    scopus 로고
    • Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: Insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder
    • R. Sultana, P. Mecocci, F. Mangialasche, R. Cecchetti, M. Baglioni, and D.A. Butterfield Increased protein and lipid oxidative damage in mitochondria isolated from lymphocytes from patients with Alzheimer's disease: insights into the role of oxidative stress in Alzheimer's disease and initial investigations into a potential biomarker for this dementing disorder J. Alzheimers Dis 24 2011 77 84
    • (2011) J. Alzheimers Dis , vol.24 , pp. 77-84
    • Sultana, R.1    Mecocci, P.2    Mangialasche, F.3    Cecchetti, R.4    Baglioni, M.5    Butterfield, D.A.6
  • 27
    • 34147143391 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from animal cells and tissue culture lines
    • F. Pallotti, and G. Lenaz Isolation and subfractionation of mitochondria from animal cells and tissue culture lines Methods Cell Biol 80 2007 3 44
    • (2007) Methods Cell Biol , vol.80 , pp. 3-44
    • Pallotti, F.1    Lenaz, G.2
  • 28
    • 13644265462 scopus 로고    scopus 로고
    • Ferulic acid ethyl ester protects neurons against amyloid β-peptide(1-42)-induced oxidative stress and neurotoxicity: Relationship to antioxidant activity
    • DOI 10.1111/j.1471-4159.2004.02899.x
    • R. Sultana, A. Ravagna, H. Mohmmad-Abdul, V. Calabrese, and D.A. Butterfield Ferulic acid ethyl ester protects neurons against amyloid beta-peptide(1-42)-induced oxidative stress and neurotoxicity: relationship to antioxidant activity J. Neurochem. 92 2005 749 758 (Pubitemid 40229546)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.4 , pp. 749-758
    • Sultana, R.1    Ravagna, A.2    Mohmmad-Abdul, H.3    Calabrese, V.4    Butterfield, D.A.5
  • 29
    • 0035857738 scopus 로고    scopus 로고
    • Protein oxidation in the brain in Alzheimer's disease
    • DOI 10.1016/S0306-4522(00)00580-7, PII S0306452200005807
    • M.Y. Aksenov, M.V. Aksenova, D.A. Butterfield, J.W. Geddes, and W.R. Markesbery Protein oxidation in the brain in Alzheimer's disease Neuroscience 103 2001 373 383 (Pubitemid 32201924)
    • (2001) Neuroscience , vol.103 , Issue.2 , pp. 373-383
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Geddes, J.W.4    Markesbery, W.R.5
  • 30
    • 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
    • DOI 10.1016/j.brainres.2007.02.084, PII S0006899307004222
    • D.A. Butterfield, T.T. Reed, M. Perluigi, C. De Marco, R. Coccia, J.N. Keller, W.R. Markesbery, and R. Sultana 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 2007 243 248 (Pubitemid 46602178)
    • (2007) Brain Research , vol.1148 , Issue.1 , 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
  • 33
    • 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
    • D.A. Butterfield, T. Reed, M. Perluigi, C. De Marco, R. Coccia, C. Cini, and R. Sultana Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment Neurosci. Lett. 397 2006 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
  • 35
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • M. Manczak, T.S. Anekonda, E. Henson, B.S. Park, J. Quinn, and P.H. Reddy Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression Hum. Mol. Genet 15 2006 1437 1449
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 36
    • 84861470082 scopus 로고    scopus 로고
    • Methionine-35 of Abeta(1-42): Importance for oxidative stress in Alzheimer disease
    • D.A. Butterfield, and R. Sultana Methionine-35 of Abeta(1-42): importance for oxidative stress in Alzheimer disease J. Amino Acids. 2011 2011 198430
    • (2011) J. Amino Acids. , vol.2011 , pp. 198430
    • Butterfield, D.A.1    Sultana, R.2
  • 37
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • D.A. Butterfield, M.L. Bader Lange, and R. Sultana Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease Biochim. Biophys. Acta 1801 2010 924 929
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 39
    • 0026547646 scopus 로고
    • Plasma concentrations of vitamins A and e and carotenoids in Alzheimer's disease
    • Z. Zaman, S. Roche, P. Fielden, P.G. Frost, D.C. Niriella, and A.C. Cayley Plasma concentrations of vitamins A and E and carotenoids in Alzheimer's disease Age Ageing 21 1992 91 94
    • (1992) Age Ageing , vol.21 , pp. 91-94
    • Zaman, Z.1    Roche, S.2    Fielden, P.3    Frost, P.G.4    Niriella, D.C.5    Cayley, A.C.6
  • 40
    • 0033744466 scopus 로고    scopus 로고
    • Mechanisms of vitamin e regulation: Research over the past decade and focus on the future
    • E. Parks, and M.G. Traber Mechanisms of vitamin E regulation: research over the past decade and focus on the future Antioxid. Redox Signaling 2 2000 405 412
    • (2000) Antioxid. Redox Signaling , vol.2 , pp. 405-412
    • Parks, E.1    Traber, M.G.2
  • 41
    • 1442314722 scopus 로고    scopus 로고
    • Early vitamin e supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease
    • S. Sung, Y. Yao, K. Uryu, H. Yang, V.M. Lee, J.Q. Trojanowski, and D. Pratico Early vitamin E supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease FASEB J 18 2004 323 325
    • (2004) FASEB J , vol.18 , pp. 323-325
    • Sung, S.1    Yao, Y.2    Uryu, K.3    Yang, H.4    Lee, V.M.5    Trojanowski, J.Q.6    Pratico, D.7
  • 43
    • 79959257484 scopus 로고    scopus 로고
    • Analysis of postmortem ventricular cerebrospinal fluid from patients with and without dementia indicates association of vitamin e with neuritic plaques and specific measures of cognitive performance
    • K. Hensley, L.L. Barnes, A. Christov, C. Tangney, W.G. Honer, J.A. Schneider, D.A. Bennett, and M.C. Morris Analysis of postmortem ventricular cerebrospinal fluid from patients with and without dementia indicates association of vitamin E with neuritic plaques and specific measures of cognitive performance J. Alzheimers Dis. 24 2011 767 774
    • (2011) J. Alzheimers Dis. , vol.24 , pp. 767-774
    • Hensley, K.1    Barnes, L.L.2    Christov, A.3    Tangney, C.4    Honer, W.G.5    Schneider, J.A.6    Bennett, D.A.7    Morris, M.C.8
  • 44
    • 0033168643 scopus 로고    scopus 로고
    • Association of antioxidants with memory in a multiethnic elderly sample using the Third National Health and Nutrition Examination survey
    • A.J. Perkins, H.C. Hendrie, C.M. Callahan, S. Gao, F.W. Unverzagt, Y. Xu, K.S. Hall, and S.L. Hui Association of antioxidants with memory in a multiethnic elderly sample using the Third National Health and Nutrition Examination Survey Am. J. Epidemiol. 150 1999 37 44 (Pubitemid 29297266)
    • (1999) American Journal of Epidemiology , vol.150 , Issue.1 , pp. 37-44
    • Perkins, A.J.1    Hendrie, H.C.2    Callahan, C.M.3    Gao, S.4    Unverzagt, F.W.5    Xu, Y.6    Hall, K.S.7    Hui, S.L.8
  • 48
    • 0027525498 scopus 로고
    • Structural and dynamic membrane properties of α-tocopherol and α- tocotrienol: Implication to the molecular mechanism of their antioxidant potency
    • DOI 10.1021/bi00091a020
    • Y.J. Suzuki, M. Tsuchiya, S.R. Wassall, Y.M. Choo, G. Govil, V.E. Kagan, and L. Packer Structural and dynamic membrane properties of alpha-tocopherol and alpha-tocotrienol: implication to the molecular mechanism of their antioxidant potency Biochemistry 32 1993 10692 10699 (Pubitemid 23327802)
    • (1993) Biochemistry , vol.32 , Issue.40 , pp. 10692-10699
    • Suzuki, Y.J.1    Tsuchiya, M.2    Wassall, S.R.3    Choo, Y.M.4    Govil, G.5    Kagan, V.E.6    Packer, L.7
  • 50
    • 35948978903 scopus 로고    scopus 로고
    • Tocopherylquinone and tocopherylhydroquinone
    • DOI 10.1179/135100007X200353
    • E. Niki Tocopherylquinone and tocopherylhydroquinone Redox Rep. 12 2007 204 210 (Pubitemid 350065107)
    • (2007) Redox Report , vol.12 , Issue.5 , pp. 204-210
    • Niki, E.1
  • 52
    • 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, R. Booze, W.R. Markesbery, and D.A. Butterfield 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 2002 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
  • 53
    • 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
    • DOI 10.1016/S0891-5849(02)00914-0, PII S0891584902009140
    • A. Castegna, M. Aksenov, M. Aksenova, V. Thongboonkerd, J.B. Klein, W.M. Pierce, R. Booze, W.R. Markesbery, and D.A. Butterfield 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 2002 562 571 (Pubitemid 34874977)
    • (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
  • 54
    • 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
    • DOI 10.1074/jbc.M314124200
    • J. Choi, A.I. Levey, S.T. Weintraub, H.D. Rees, M. Gearing, L.S. Chin, and 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 (Pubitemid 38445905)
    • (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
  • 56
    • 75149118997 scopus 로고    scopus 로고
    • Role of oxidative stress in the progression of Alzheimer's disease
    • R. Sultana, and D.A. Butterfield Role of oxidative stress in the progression of Alzheimer's disease J. Alzheimers Dis. 19 2010 341 353
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 341-353
    • Sultana, R.1    Butterfield, D.A.2
  • 57
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: Many pathways to neurodegeneration
    • D.A. Butterfield, S.S. Hardas, and M.L. Lange Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration J. Alzheimers Dis. 20 2010 369 393
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.3
  • 59
    • 39749136069 scopus 로고    scopus 로고
    • Vimentin supports mitochondrial morphology and organization
    • DOI 10.1042/BJ20071072
    • H.L. Tang, H.L. Lung, K.C. Wu, A.H. Le, H.M. Tang, and M.C. Fung Vimentin supports mitochondrial morphology and organization Biochem. J. 410 2008 141 146 (Pubitemid 351300333)
    • (2008) Biochemical Journal , vol.410 , Issue.1 , pp. 141-146
    • Tang, H.L.1    Lung, H.L.2    Wu, K.C.3    Le, A.-H.P.4    Tang, H.M.5    Fung, M.C.6
  • 60
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
    • DOI 10.1179/135100002125000352
    • J. Fujii, and Y. Ikeda Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein Redox Rep. 7 2002 123 130 (Pubitemid 34700435)
    • (2002) Redox Report , vol.7 , Issue.3 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 62
    • 77956250065 scopus 로고    scopus 로고
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system J. Biol. Chem. 285 2010 27850 27858
    • (2010) J. Biol. Chem. , vol.285 , pp. 27850-27858
    • Drechsel, D.A.1    Patel, M.2
  • 63
    • 84870584588 scopus 로고    scopus 로고
    • Thioredoxin reductase deficiency potentiates oxidative stress, mitochondrial dysfunction and cell death in dopaminergic cells
    • P. Lopert, B.J. Day, and M. Patel Thioredoxin reductase deficiency potentiates oxidative stress, mitochondrial dysfunction and cell death in dopaminergic cells PLoS One 7 2012 e50683
    • (2012) PLoS One , vol.7 , pp. 50683
    • Lopert, P.1    Day, B.J.2    Patel, M.3
  • 64
    • 0035233637 scopus 로고    scopus 로고
    • Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down Syndrome
    • S.H. Kim, M. Fountoulakis, N. Cairns, and G. Lubec Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome J. Neural Transm. Suppl. 61 2001 223 235 (Pubitemid 38085085)
    • (2001) Journal of Neural Transmission, Supplement , Issue.61 , pp. 223-235
    • Kim, S.H.1    Fountoulakis, M.2    Cairns, N.3    Lubec, G.4
  • 65
    • 4744373181 scopus 로고    scopus 로고
    • Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
    • DOI 10.1074/jbc.M407707200
    • T.S. Chang, C.S. Cho, S. Park, S. Yu, S.W. Kang, and S.G. Rhee Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria J. Biol. Chem. 279 2004 41975 41984 (Pubitemid 39313648)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41975-41984
    • Chang, T.-S.1    Cho, C.-S.2    Park, S.3    Yu, S.4    Sang, W.K.5    Sue, G.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.