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Volumn 8, Issue 1, 2009, Pages 1-17

Proteomics in animal models of Alzheimer's and Parkinson's diseases

Author keywords

Alzheimer's disease; Animal models; Parkinson's disease; Proteomics

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; DJ 1 PROTEIN; DOPAMINE; GLYCOGEN SYNTHASE KINASE 3BETA; LEUCINE RICH REPEAT KINASE 2; PARKIN; PHOSPHOTRANSFERASE; PRESENILIN 1; PRESENILIN 2; PTEN INDUCED PUTATIVE KINASE 1; QUINONE DERIVATIVE; TAU PROTEIN; UBIQUITIN CARBOXY TERMINAL HYDROLASE L1; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 57749184790     PISSN: 15681637     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.arr.2008.07.003     Document Type: Short Survey
Times cited : (72)

References (120)
  • 3
    • 0034751077 scopus 로고    scopus 로고
    • Neurofilament proteins NF-L, NF-M and NF-H in brain of patients with Down syndrome and Alzheimer's disease
    • Bajo M., Yoo B.C., Cairns N., Gratzer M., and Lubec G. Neurofilament proteins NF-L, NF-M and NF-H in brain of patients with Down syndrome and Alzheimer's disease. Amino Acids 21 3 (2001) 293-301
    • (2001) Amino Acids , vol.21 , Issue.3 , pp. 293-301
    • Bajo, M.1    Yoo, B.C.2    Cairns, N.3    Gratzer, M.4    Lubec, G.5
  • 4
    • 0032842038 scopus 로고    scopus 로고
    • Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease
    • Berman S.B., and Hastings T.G. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease. J. Neurochem. 73 3 (1999) 1127-1137
    • (1999) J. Neurochem. , vol.73 , Issue.3 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 5
    • 0023731159 scopus 로고
    • Familial Alzheimer's disease in American descendants of the Volga Germans: probable genetic founder effect
    • Bird T.D., Lampe T.H., Nemens E.J., Miner G.W., Sumi S.M., and Schellenberg G.D. Familial Alzheimer's disease in American descendants of the Volga Germans: probable genetic founder effect. Ann. Neurol. 23 1 (1988) 25-31
    • (1988) Ann. Neurol. , vol.23 , Issue.1 , pp. 25-31
    • Bird, T.D.1    Lampe, T.H.2    Nemens, E.J.3    Miner, G.W.4    Sumi, S.M.5    Schellenberg, G.D.6
  • 7
    • 33745990556 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease
    • Boyd-Kimball D., Poon H.F., Lynn B.C., Cai J., Pierce Jr. W.M., Klein J.B., Ferguson J., Link C.D., and Butterfield D.A. Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease. Neurobiol. Aging 27 9 (2006) 1239-1249
    • (2006) Neurobiol. Aging , vol.27 , Issue.9 , pp. 1239-1249
    • Boyd-Kimball, D.1    Poon, H.F.2    Lynn, B.C.3    Cai, J.4    Pierce Jr., W.M.5    Klein, J.B.6    Ferguson, J.7    Link, C.D.8    Butterfield, D.A.9
  • 8
    • 15744387176 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: implications for Alzheimer's disease
    • Boyd-Kimball D., Sultana R., Poon H.F., Lynn B.C., Casamenti F., Pepeu G., Klein J.B., and Butterfield D.A. Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: implications for Alzheimer's disease. Neuroscience 132 2 (2005) 313-324
    • (2005) Neuroscience , vol.132 , Issue.2 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Poon, H.F.3    Lynn, B.C.4    Casamenti, F.5    Pepeu, G.6    Klein, J.B.7    Butterfield, D.A.8
  • 9
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H., and Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82 4 (1991) 239-259
    • (1991) Acta Neuropathol. , vol.82 , Issue.4 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 10
    • 0027406083 scopus 로고
    • Motor neurons and neurofilaments in sickness and in health
    • Brady S.T. Motor neurons and neurofilaments in sickness and in health. Cell 73 1 (1993) 1-3
    • (1993) Cell , vol.73 , Issue.1 , pp. 1-3
    • Brady, S.T.1
  • 11
    • 0020355825 scopus 로고
    • Studies of familial type III hyperlipoproteinemia using as a genetic marker the apoE phenotype E2/2
    • Breslow J.L., Zannis V.I., SanGiacomo T.R., Third J.L., Tracy T., and Glueck C.J. Studies of familial type III hyperlipoproteinemia using as a genetic marker the apoE phenotype E2/2. J. Lipid Res. 23 8 (1982) 1224-1235
    • (1982) J. Lipid Res. , vol.23 , Issue.8 , pp. 1224-1235
    • Breslow, J.L.1    Zannis, V.I.2    SanGiacomo, T.R.3    Third, J.L.4    Tracy, T.5    Glueck, C.J.6
  • 12
    • 0030919274 scopus 로고    scopus 로고
    • Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-gamma and aldolase C
    • Bulliard C., Zurbriggen R., Tornare J., Faty M., Dastoor Z., and Dreyer J.L. Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-gamma and aldolase C. Biochem. J. 324 Pt 2 (1997) 555-563
    • (1997) Biochem. J. , vol.324 , Issue.PART 2 , pp. 555-563
    • Bulliard, C.1    Zurbriggen, R.2    Tornare, J.3    Faty, M.4    Dastoor, Z.5    Dreyer, J.L.6
  • 13
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: a new approach to investigate oxidative stress in Alzheimer's disease brain
    • Butterfield D.A. Proteomics: a new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 1000 1-2 (2004) 1-7
    • (2004) Brain Res. , vol.1000 , Issue.1-2 , pp. 1-7
    • Butterfield, D.A.1
  • 14
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide
    • Butterfield D.A., Drake J., Pocernich C., and Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 7 12 (2001) 548-554
    • (2001) Trends Mol. Med. , vol.7 , Issue.12 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 15
    • 33847069643 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment
    • Butterfield D.A., Gnjec A., Poon H.F., Castegna A., Pierce W.M., Klein J.B., and Martins R.N. Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment. J. Alzheimers Dis. 10 4 (2006) 391-397
    • (2006) J. Alzheimers Dis. , vol.10 , Issue.4 , 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
  • 16
    • 0030921729 scopus 로고    scopus 로고
    • Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer's disease
    • Butterfield D.A., Hensley K., Cole P., Subramaniam R., Aksenov M., Aksenova M., Bummer P.M., Haley B.E., and Carney J.M. Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer's disease. J. Neurochem. 68 6 (1997) 2451-2457
    • (1997) J. Neurochem. , vol.68 , Issue.6 , pp. 2451-2457
    • Butterfield, D.A.1    Hensley, K.2    Cole, P.3    Subramaniam, R.4    Aksenov, M.5    Aksenova, M.6    Bummer, P.M.7    Haley, B.E.8    Carney, J.M.9
  • 17
    • 26244456297 scopus 로고    scopus 로고
    • The senescence-accelerated prone mouse (SAMP8): a model of age-related cognitive decline with relevance to alterations of the gene expression and protein abnormalities in Alzheimer's disease
    • Butterfield D.A., and Poon H.F. The senescence-accelerated prone mouse (SAMP8): a model of age-related cognitive decline with relevance to alterations of the gene expression and protein abnormalities in Alzheimer's disease. Exp. Gerontol. 40 10 (2005) 774-783
    • (2005) Exp. Gerontol. , vol.40 , Issue.10 , pp. 774-783
    • Butterfield, D.A.1    Poon, H.F.2
  • 18
    • 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 D.A., Reed T., Newman S.F., and Sultana R. 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 5 (2007) 658-677
    • (2007) Free Radic. Biol. Med. , vol.43 , Issue.5 , pp. 658-677
    • Butterfield, D.A.1    Reed, T.2    Newman, S.F.3    Sultana, R.4
  • 19
    • 0032587025 scopus 로고    scopus 로고
    • Interleukin-1beta activates forebrain glial cells and increases nitric oxide production and cortical glutamate and GABA release in vivo: implications for Alzheimer's disease
    • Casamenti F., Prosperi C., Scali C., Giovannelli L., Colivicchi M.A., Faussone-Pellegrini M.S., and Pepeu G. Interleukin-1beta activates forebrain glial cells and increases nitric oxide production and cortical glutamate and GABA release in vivo: implications for Alzheimer's disease. Neuroscience 91 3 (1999) 831-842
    • (1999) Neuroscience , vol.91 , Issue.3 , pp. 831-842
    • Casamenti, F.1    Prosperi, C.2    Scali, C.3    Giovannelli, L.4    Colivicchi, M.A.5    Faussone-Pellegrini, M.S.6    Pepeu, G.7
  • 20
    • 1842528400 scopus 로고    scopus 로고
    • Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins
    • Casserly I., and Topol E. Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins. Lancet 363 9415 (2004) 1139-1146
    • (2004) Lancet , vol.363 , Issue.9415 , pp. 1139-1146
    • Casserly, I.1    Topol, E.2
  • 21
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. 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) 562-571
    • (2002) Free Radic. Biol. Med. , 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
  • 22
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II. Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. 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) 1524-1532
    • (2002) J. Neurochem. , vol.82 , Issue.6 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 23
    • 33646796739 scopus 로고    scopus 로고
    • In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease
    • Chinta S.J., Rajagopalan S., Butterfield D.A., and Andersen J.K. In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease. Neurosci. Lett. 402 1-2 (2006) 137-141
    • (2006) Neurosci. Lett. , vol.402 , Issue.1-2 , pp. 137-141
    • Chinta, S.J.1    Rajagopalan, S.2    Butterfield, D.A.3    Andersen, J.K.4
  • 25
    • 33846019607 scopus 로고    scopus 로고
    • Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes
    • David D.C., Ittner L.M., Gehrig P., Nergenau D., Shepherd C., Halliday G., and Gotz J. Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes. Proteomics 6 24 (2006) 6566-6577
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6566-6577
    • David, D.C.1    Ittner, L.M.2    Gehrig, P.3    Nergenau, D.4    Shepherd, C.5    Halliday, G.6    Gotz, J.7
  • 26
    • 0036829946 scopus 로고    scopus 로고
    • Neuroprotective and neurorestorative strategies for Parkinson's disease
    • Dawson T.M., and Dawson V.L. Neuroprotective and neurorestorative strategies for Parkinson's disease. Nat. Neurosci. 5 Suppl. (2002) 1058-1061
    • (2002) Nat. Neurosci. , vol.5 , Issue.SUPPL , pp. 1058-1061
    • Dawson, T.M.1    Dawson, V.L.2
  • 27
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson T.M., and Dawson V.L. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302 5646 (2003) 819-822
    • (2003) Science , vol.302 , Issue.5646 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 28
    • 0026041203 scopus 로고
    • Coronin, an actin binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein beta subunits
    • de Hostos E.L., Bradtke B., Lottspeich F., Guggenheim R., and Gerisch G. Coronin, an actin binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein beta subunits. EMBO J. 10 13 (1991) 4097-4104
    • (1991) EMBO J. , vol.10 , Issue.13 , pp. 4097-4104
    • de Hostos, E.L.1    Bradtke, B.2    Lottspeich, F.3    Guggenheim, R.4    Gerisch, G.5
  • 29
    • 21244475585 scopus 로고    scopus 로고
    • A proteomic approach in the study of an animal model of Parkinson's disease
    • De Iuliis A., Grigoletto J., Recchia A., Giusti P., and Arslan P. A proteomic approach in the study of an animal model of Parkinson's disease. Clin. Chim. Acta 357 2 (2005) 202-209
    • (2005) Clin. Chim. Acta , vol.357 , Issue.2 , pp. 202-209
    • De Iuliis, A.1    Grigoletto, J.2    Recchia, A.3    Giusti, P.4    Arslan, P.5
  • 31
    • 41549132572 scopus 로고    scopus 로고
    • Proteome analysis of ventral midbrain in MPTP-treated normal and L1cam transgenic mice
    • Diedrich M., Mao L., Bernreuther C., Zabel C., Nebrich G., Kleene R., and Klose J. Proteome analysis of ventral midbrain in MPTP-treated normal and L1cam transgenic mice. Proteomics 8 6 (2008) 1266-1275
    • (2008) Proteomics , vol.8 , Issue.6 , pp. 1266-1275
    • Diedrich, M.1    Mao, L.2    Bernreuther, C.3    Zabel, C.4    Nebrich, G.5    Kleene, R.6    Klose, J.7
  • 32
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty M.K., and Morrison D.K. Unlocking the code of 14-3-3. J. Cell Sci. 117 Pt 10 (2004) 1875-1884
    • (2004) J. Cell Sci. , vol.117 , Issue.PART 10 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 33
    • 0037342554 scopus 로고    scopus 로고
    • The antioxidants alpha-lipoic acid and N-acetylcysteine reverse memory impairment and brain oxidative stress in aged SAMP8 mice
    • Farr S.A., Poon H.F., Dogrukol-Ak D., Drake J., Banks W.A., Eyerman E., Butterfield D.A., and Morley J.E. The antioxidants alpha-lipoic acid and N-acetylcysteine reverse memory impairment and brain oxidative stress in aged SAMP8 mice. J. Neurochem. 84 5 (2003) 1173-1183
    • (2003) J. Neurochem. , vol.84 , Issue.5 , pp. 1173-1183
    • Farr, S.A.1    Poon, H.F.2    Dogrukol-Ak, D.3    Drake, J.4    Banks, W.A.5    Eyerman, E.6    Butterfield, D.A.7    Morley, J.E.8
  • 35
    • 0025954066 scopus 로고
    • Ageing and Parkinson's disease: substantia nigra regional selectivity
    • Fearnley J.M., and Lees A.J. Ageing and Parkinson's disease: substantia nigra regional selectivity. Brain 114 Pt 5 (1991) 2283-2301
    • (1991) Brain , vol.114 , Issue.PART 5 , pp. 2283-2301
    • Fearnley, J.M.1    Lees, A.J.2
  • 36
    • 0344653645 scopus 로고    scopus 로고
    • Learning and memory in the SAMP8 mouse
    • Flood J.F., and Morley J.E. Learning and memory in the SAMP8 mouse. Neurosci. Biobehav. Rev. 22 1 (1998) 1-20
    • (1998) Neurosci. Biobehav. Rev. , vol.22 , Issue.1 , pp. 1-20
    • Flood, J.F.1    Morley, J.E.2
  • 39
    • 0023233199 scopus 로고
    • The use of the MPTP-treated mouse as an animal model of parkinsonism
    • Heikkila R.E., and Sonsalla P.K. The use of the MPTP-treated mouse as an animal model of parkinsonism. Can. J. Neurol. Sci. 14 3 Suppl. (1987) 436-440
    • (1987) Can. J. Neurol. Sci. , vol.14 , Issue.3 SUPPL , pp. 436-440
    • Heikkila, R.E.1    Sonsalla, P.K.2
  • 42
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao K., Chapman P., Nilsen S., Eckman C., Harigaya Y., Younkin S., Yang F., and Cole G. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 274 5284 (1996) 99-102
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 43
    • 0037378023 scopus 로고    scopus 로고
    • Neuroinflammatory processes in Parkinson's disease
    • (discussion S58-60)
    • Hunot S., and Hirsch E.C. Neuroinflammatory processes in Parkinson's disease. Ann. Neurol. 53 Suppl. 3 (2003) S49-S58 (discussion S58-60)
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Hunot, S.1    Hirsch, E.C.2
  • 44
    • 41549097831 scopus 로고    scopus 로고
    • Proteomics of Caenorhabditis elegans over-expressing human alpha-synuclein analyzed by fluorogenic derivatization-liquid chromatography/tandem mass spectrometry: identification of actin and several ribosomal proteins as negative markers at early Parkinson's disease stages
    • Ichibangase T., Saimaru H., Takamura N., Kuwahara T., Koyama A., Iwatsubo T., and Imai K. Proteomics of Caenorhabditis elegans over-expressing human alpha-synuclein analyzed by fluorogenic derivatization-liquid chromatography/tandem mass spectrometry: identification of actin and several ribosomal proteins as negative markers at early Parkinson's disease stages. Biomed. Chromatogr. 22 3 (2008) 232-234
    • (2008) Biomed. Chromatogr. , vol.22 , Issue.3 , pp. 232-234
    • Ichibangase, T.1    Saimaru, H.2    Takamura, N.3    Kuwahara, T.4    Koyama, A.5    Iwatsubo, T.6    Imai, K.7
  • 45
    • 0026480277 scopus 로고
    • Age-related changes in radial-arm maze learning and basal forebrain cholinergic systems in senescence accelerated mice (SAM)
    • Ikegami S., Shumiya S., and Kawamura H. Age-related changes in radial-arm maze learning and basal forebrain cholinergic systems in senescence accelerated mice (SAM). Behav. Brain Res. 51 1 (1992) 15-22
    • (1992) Behav. Brain Res. , vol.51 , Issue.1 , pp. 15-22
    • Ikegami, S.1    Shumiya, S.2    Kawamura, H.3
  • 46
    • 15544374722 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease
    • Jin J., Meredith G.E., Chen L., Zhou Y., Xu J., Shie F.S., Lockhart P., and Zhang J. Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease. Brain Res. Mol. Brain Res. 134 1 (2005) 119-138
    • (2005) Brain Res. Mol. Brain Res. , vol.134 , Issue.1 , pp. 119-138
    • Jin, J.1    Meredith, G.E.2    Chen, L.3    Zhou, Y.4    Xu, J.5    Shie, F.S.6    Lockhart, P.7    Zhang, J.8
  • 47
    • 0026778866 scopus 로고
    • Dihydrolipoic acid-a universal antioxidant both in the membrane and in the aqueous phase. Reduction of peroxyl, ascorbyl and chromanoxyl radicals
    • Kagan V.E., Shvedova A., Serbinova E., Khan S., Swanson C., Powell R., and Packer L. Dihydrolipoic acid-a universal antioxidant both in the membrane and in the aqueous phase. Reduction of peroxyl, ascorbyl and chromanoxyl radicals. Biochem. Pharmacol. 44 8 (1992) 1637-1649
    • (1992) Biochem. Pharmacol. , vol.44 , Issue.8 , pp. 1637-1649
    • Kagan, V.E.1    Shvedova, A.2    Serbinova, E.3    Khan, S.4    Swanson, C.5    Powell, R.6    Packer, L.7
  • 49
    • 0035577280 scopus 로고    scopus 로고
    • Altered brain phosphocreatine and ATP regulation when mitochondrial creatine kinase is absent
    • Kekelidze T., Khait I., Togliatti A., Benzecry J.M., Wieringa B., and Holtzman D. Altered brain phosphocreatine and ATP regulation when mitochondrial creatine kinase is absent. J. Neurosci. Res. 66 5 (2001) 866-872
    • (2001) J. Neurosci. Res. , vol.66 , Issue.5 , pp. 866-872
    • Kekelidze, T.1    Khait, I.2    Togliatti, A.3    Benzecry, J.M.4    Wieringa, B.5    Holtzman, D.6
  • 51
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome
    • Klose J., and Kobalz U. Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis 16 6 (1995) 1034-1059
    • (1995) Electrophoresis , vol.16 , Issue.6 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 53
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson's disease. First of two parts
    • Lang A.E., and Lozano A.M. Parkinson's disease. First of two parts. N. Engl. J. Med. 339 15 (1998) 1044-1053
    • (1998) N. Engl. J. Med. , vol.339 , Issue.15 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 54
    • 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 C.M., Hackett J.M., Huang F.F., Keller J.N., Szweda L.I., Markesbery W.R., and Butterfield D.A. 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 2 (2001) 413-416
    • (2001) J. Neurochem. , vol.78 , Issue.2 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3    Keller, J.N.4    Szweda, L.I.5    Markesbery, W.R.6    Butterfield, D.A.7
  • 55
    • 0026569053 scopus 로고
    • When did Ray Kennedy's Parkinson's disease begin?
    • Lees A.J. When did Ray Kennedy's Parkinson's disease begin?. Mov. Disord. 7 2 (1992) 110-116
    • (1992) Mov. Disord. , vol.7 , Issue.2 , pp. 110-116
    • Lees, A.J.1
  • 57
    • 22544465257 scopus 로고    scopus 로고
    • LRRK2 haplotype analyses in European and North African families with Parkinson disease: a common founder for the G2019S mutation dating from the 13th century
    • Lesage S., Leutenegger A.L., Ibanez P., Janin S., Lohmann E., Durr A., and Brice A. LRRK2 haplotype analyses in European and North African families with Parkinson disease: a common founder for the G2019S mutation dating from the 13th century. Am. J. Hum. Genet. 77 2 (2005) 330-332
    • (2005) Am. J. Hum. Genet. , vol.77 , Issue.2 , pp. 330-332
    • Lesage, S.1    Leutenegger, A.L.2    Ibanez, P.3    Janin, S.4    Lohmann, E.5    Durr, A.6    Brice, A.7
  • 59
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein
    • Lotharius J., and Brundin P. Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein. Nat. Rev. Neurosci. 3 12 (2002) 932-942
    • (2002) Nat. Rev. Neurosci. , vol.3 , Issue.12 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 60
    • 0033600301 scopus 로고    scopus 로고
    • Molecular basis of the neurodegenerative disorders
    • Martin J.B. Molecular basis of the neurodegenerative disorders. N. Engl. J. Med. 340 25 (1999) 1970-1980
    • (1999) N. Engl. J. Med. , vol.340 , Issue.25 , pp. 1970-1980
    • Martin, J.B.1
  • 61
    • 33646011523 scopus 로고    scopus 로고
    • Proteomic analysis of microglial contribution to mouse strain-dependent dopaminergic neurotoxicity
    • McLaughlin P., Zhou Y., Ma T., Liu J., Zhang W., Hong J.S., Kovacs M., and Zhang J. Proteomic analysis of microglial contribution to mouse strain-dependent dopaminergic neurotoxicity. Glia 53 6 (2006) 567-582
    • (2006) Glia , vol.53 , Issue.6 , pp. 567-582
    • McLaughlin, P.1    Zhou, Y.2    Ma, T.3    Liu, J.4    Zhang, W.5    Hong, J.S.6    Kovacs, M.7    Zhang, J.8
  • 62
    • 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
    • Mirra S.S., Heyman A., McKeel D., Sumi S.M., Crain B.J., Brownlee L.M., Vogel F.S., Hughes J.P., van Belle G., and Berg L. 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    Vogel, F.S.7    Hughes, J.P.8    van Belle, G.9    Berg, L.10
  • 64
    • 0036294296 scopus 로고    scopus 로고
    • Antibody to amyloid beta protein alleviates impaired acquisition, retention, and memory processing in SAMP8 mice
    • Morley J.E., Farr S.A., and Flood J.F. Antibody to amyloid beta protein alleviates impaired acquisition, retention, and memory processing in SAMP8 mice. Neurobiol. Learn. Mem. 78 1 (2002) 125-138
    • (2002) Neurobiol. Learn. Mem. , vol.78 , Issue.1 , pp. 125-138
    • Morley, J.E.1    Farr, S.A.2    Flood, J.F.3
  • 65
    • 24344446871 scopus 로고    scopus 로고
    • Clinical practice. Diagnosis and initial management of Parkinson's disease
    • Nutt J.G., and Wooten G.F. Clinical practice. Diagnosis and initial management of Parkinson's disease. N. Engl. J. Med. 353 10 (2005) 1021-1027
    • (2005) N. Engl. J. Med. , vol.353 , Issue.10 , pp. 1021-1027
    • Nutt, J.G.1    Wooten, G.F.2
  • 66
    • 0023100407 scopus 로고
    • MPTP-induced parkinsonian model in mice: biochemistry, pharmacology and behavior
    • Ogawa N., Mizukawa K., Hirose Y., Kajita S., Ohara S., and Watanabe Y. MPTP-induced parkinsonian model in mice: biochemistry, pharmacology and behavior. Eur. Neurol. 26 Suppl. 1 (1987) 16-23
    • (1987) Eur. Neurol. , vol.26 , Issue.SUPPL. 1 , pp. 16-23
    • Ogawa, N.1    Mizukawa, K.2    Hirose, Y.3    Kajita, S.4    Ohara, S.5    Watanabe, Y.6
  • 68
    • 0029031443 scopus 로고
    • Thioctic (lipoic) acid: a therapeutic metal-chelating antioxidant?
    • Ou P., Tritschler H.J., and Wolff S.P. Thioctic (lipoic) acid: a therapeutic metal-chelating antioxidant?. Biochem. Pharmacol. 50 1 (1995) 123-126
    • (1995) Biochem. Pharmacol. , vol.50 , Issue.1 , pp. 123-126
    • Ou, P.1    Tritschler, H.J.2    Wolff, S.P.3
  • 70
    • 1342264250 scopus 로고    scopus 로고
    • Parkinson's disease, pesticides and individual vulnerability
    • Paolini M., Sapone A., and Gonzalez F.J. Parkinson's disease, pesticides and individual vulnerability. Trends Pharmacol. Sci. 25 3 (2004) 124-129
    • (2004) Trends Pharmacol. Sci. , vol.25 , Issue.3 , pp. 124-129
    • Paolini, M.1    Sapone, A.2    Gonzalez, F.J.3
  • 72
    • 28844439032 scopus 로고    scopus 로고
    • Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function
    • Periquet M., Corti O., Jacquier S., and Brice A. Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J. Neurochem. 95 5 (2005) 1259-1276
    • (2005) J. Neurochem. , vol.95 , Issue.5 , pp. 1259-1276
    • Periquet, M.1    Corti, O.2    Jacquier, S.3    Brice, A.4
  • 73
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 18 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 75
    • 2942659505 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain
    • Poon H.F., Castegna A., Farr S.A., Thongboonkerd V., Lynn B.C., Banks W.A., Morley J.E., Klein J.B., and Butterfield D.A. Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain. Neuroscience 126 4 (2004) 915-926
    • (2004) Neuroscience , vol.126 , Issue.4 , pp. 915-926
    • Poon, H.F.1    Castegna, A.2    Farr, S.A.3    Thongboonkerd, V.4    Lynn, B.C.5    Banks, W.A.6    Morley, J.E.7    Klein, J.B.8    Butterfield, D.A.9
  • 76
    • 22744455017 scopus 로고    scopus 로고
    • Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein
    • Poon H.F., Farr S.A., Banks W.A., Pierce W.M., Klein J.B., Morley J.E., and Butterfield D.A. Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein. Brain Res. Mol. Brain Res. 138 1 (2005) 8-16
    • (2005) Brain Res. Mol. Brain Res. , vol.138 , Issue.1 , pp. 8-16
    • Poon, H.F.1    Farr, S.A.2    Banks, W.A.3    Pierce, W.M.4    Klein, J.B.5    Morley, J.E.6    Butterfield, D.A.7
  • 77
    • 14544284095 scopus 로고    scopus 로고
    • Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: implications for aging and age-related neurodegenerative disorders
    • Poon H.F., Farr S.A., Thongboonkerd V., Lynn B.C., Banks W.A., Morley J.E., Klein J.B., and Butterfield D.A. Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: implications for aging and age-related neurodegenerative disorders. Neurochem. Int. 46 2 (2005) 159-168
    • (2005) Neurochem. Int. , vol.46 , Issue.2 , pp. 159-168
    • Poon, H.F.1    Farr, S.A.2    Thongboonkerd, V.3    Lynn, B.C.4    Banks, W.A.5    Morley, J.E.6    Klein, J.B.7    Butterfield, D.A.8
  • 78
    • 14744305520 scopus 로고    scopus 로고
    • Mitochondrial associated metabolic proteins are selectively oxidized in A30P alpha-synuclein transgenic mice-a model of familial Parkinson's disease
    • Poon H.F., Frasier M., Shreve N., Calabrese V., Wolozin B., and Butterfield D.A. Mitochondrial associated metabolic proteins are selectively oxidized in A30P alpha-synuclein transgenic mice-a model of familial Parkinson's disease. Neurobiol. Dis. 18 3 (2005) 492-498
    • (2005) Neurobiol. Dis. , vol.18 , Issue.3 , pp. 492-498
    • Poon, H.F.1    Frasier, M.2    Shreve, N.3    Calabrese, V.4    Wolozin, B.5    Butterfield, D.A.6
  • 79
    • 3242715959 scopus 로고    scopus 로고
    • Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice
    • Poon H.F., Joshi G., Sultana R., Farr S.A., Banks W.A., Morley J.E., Calabrese V., and Butterfield D.A. Antisense directed at the Abeta region of APP decreases brain oxidative markers in aged senescence accelerated mice. Brain Res. 1018 1 (2004) 86-96
    • (2004) Brain Res. , vol.1018 , Issue.1 , pp. 86-96
    • Poon, H.F.1    Joshi, G.2    Sultana, R.3    Farr, S.A.4    Banks, W.A.5    Morley, J.E.6    Calabrese, V.7    Butterfield, D.A.8
  • 80
    • 0347379936 scopus 로고    scopus 로고
    • A new role for IQ motif proteins in regulating calmodulin function
    • Putkey J.A., Kleerekoper Q., Gaertner T.R., and Waxham M.N. A new role for IQ motif proteins in regulating calmodulin function. J. Biol. Chem. 278 50 (2003) 49667-49670
    • (2003) J. Biol. Chem. , vol.278 , Issue.50 , pp. 49667-49670
    • Putkey, J.A.1    Kleerekoper, Q.2    Gaertner, T.R.3    Waxham, M.N.4
  • 81
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains
    • Rabilloud T. Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics 2 1 (2002) 3-10
    • (2002) Proteomics , vol.2 , Issue.1 , pp. 3-10
    • Rabilloud, T.1
  • 83
    • 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 W.M., Klein J.B., Turner D.M., Coccia R., Markesbery W.R., and Butterfield D.A. 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 1 (2008) 107-120
    • (2008) Neurobiol. Dis. , vol.30 , Issue.1 , 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
  • 85
    • 36849010801 scopus 로고    scopus 로고
    • Proteomic identification of biomarkers in the cerebrospinal fluid in a rat model of nigrostriatal dopaminergic degeneration
    • Rite I., Arguelles S., Venero J.L., Garcia-Rodriguez S., Ayala A., Cano J., and Machado A. Proteomic identification of biomarkers in the cerebrospinal fluid in a rat model of nigrostriatal dopaminergic degeneration. J. Neurosci. Res. 85 16 (2007) 3607-3618
    • (2007) J. Neurosci. Res. , vol.85 , Issue.16 , pp. 3607-3618
    • Rite, I.1    Arguelles, S.2    Venero, J.L.3    Garcia-Rodriguez, S.4    Ayala, A.5    Cano, J.6    Machado, A.7
  • 86
    • 0038240721 scopus 로고    scopus 로고
    • Causative and susceptibility genes for Alzheimer's disease: a review
    • Rocchi A., Pellegrini S., Siciliano G., and Murri L. Causative and susceptibility genes for Alzheimer's disease: a review. Brain Res. Bull. 61 1 (2003) 1-24
    • (2003) Brain Res. Bull. , vol.61 , Issue.1 , pp. 1-24
    • Rocchi, A.1    Pellegrini, S.2    Siciliano, G.3    Murri, L.4
  • 88
    • 33745847479 scopus 로고    scopus 로고
    • Diagnosis and treatment of Parkinson disease: molecules to medicine
    • Savitt J.M., Dawson V.L., and Dawson T.M. Diagnosis and treatment of Parkinson disease: molecules to medicine. J. Clin. Invest. 116 7 (2006) 1744-1754
    • (2006) J. Clin. Invest. , vol.116 , Issue.7 , pp. 1744-1754
    • Savitt, J.M.1    Dawson, V.L.2    Dawson, T.M.3
  • 90
    • 0035656206 scopus 로고    scopus 로고
    • Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process
    • Schonberger S.J., Edgar P.F., Kydd R., Faull R.L., and Cooper G.J. Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process. Proteomics 1 12 (2001) 1519-1528
    • (2001) Proteomics , vol.1 , Issue.12 , pp. 1519-1528
    • Schonberger, S.J.1    Edgar, P.F.2    Kydd, R.3    Faull, R.L.4    Cooper, G.J.5
  • 91
    • 0030938846 scopus 로고    scopus 로고
    • Regulation of cellular thiols in human lymphocytes by alpha-lipoic acid: a flow cytometric analysis
    • Sen C.K., Roy S., Han D., and Packer L. Regulation of cellular thiols in human lymphocytes by alpha-lipoic acid: a flow cytometric analysis. Free Radic. Biol. Med. 22 7 (1997) 1241-1257
    • (1997) Free Radic. Biol. Med. , vol.22 , Issue.7 , pp. 1241-1257
    • Sen, C.K.1    Roy, S.2    Han, D.3    Packer, L.4
  • 94
    • 8744315404 scopus 로고    scopus 로고
    • Profiling proteins related to amyloid deposited brain of Tg2576 mice
    • Shin S.J., Lee S.E., Boo J.H., Kim M., Yoon Y.D., Kim S.I., and Mook-Jung I. Profiling proteins related to amyloid deposited brain of Tg2576 mice. Proteomics 4 11 (2004) 3359-3368
    • (2004) Proteomics , vol.4 , Issue.11 , pp. 3359-3368
    • Shin, S.J.1    Lee, S.E.2    Boo, J.H.3    Kim, M.4    Yoon, Y.D.5    Kim, S.I.6    Mook-Jung, I.7
  • 97
    • 0035477025 scopus 로고    scopus 로고
    • Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis
    • Smolka M.B., Zhou H., Purkayastha S., and Aebersold R. Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis. Anal. Biochem. 297 1 (2001) 25-31
    • (2001) Anal. Biochem. , vol.297 , Issue.1 , pp. 25-31
    • Smolka, M.B.1    Zhou, H.2    Purkayastha, S.3    Aebersold, R.4
  • 98
    • 0035097503 scopus 로고    scopus 로고
    • Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation
    • Spira P.J., Sharpe D.M., Halliday G., Cavanagh J., and Nicholson G.A. Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation. Ann. Neurol. 49 3 (2001) 313-319
    • (2001) Ann. Neurol. , vol.49 , Issue.3 , pp. 313-319
    • Spira, P.J.1    Sharpe, D.M.2    Halliday, G.3    Cavanagh, J.4    Nicholson, G.A.5
  • 102
    • 0036807924 scopus 로고    scopus 로고
    • Proteomic profiling and neurodegeneration in Alzheimer's disease
    • Tsuji T., Shiozaki A., Kohno R., Yoshizato K., and Shimohama S. 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
  • 105
    • 39249083911 scopus 로고    scopus 로고
    • Proteomic analysis of rat brain mitochondria following exposure to dopamine quinone: implications for Parkinson disease
    • Van Laar V.S., Dukes A.A., Cascio M., and Hastings T.G. Proteomic analysis of rat brain mitochondria following exposure to dopamine quinone: implications for Parkinson disease. Neurobiol. Dis. 29 3 (2008) 477-489
    • (2008) Neurobiol. Dis. , vol.29 , Issue.3 , pp. 477-489
    • Van Laar, V.S.1    Dukes, A.A.2    Cascio, M.3    Hastings, T.G.4
  • 106
    • 0031011896 scopus 로고    scopus 로고
    • Time course changes in the dopaminergic nigrostriatal system following transection of the medial forebrain bundle: detection of oxidatively modified proteins in substantia nigra
    • Venero J.L., Revuelta M., Cano J., and Machado A. Time course changes in the dopaminergic nigrostriatal system following transection of the medial forebrain bundle: detection of oxidatively modified proteins in substantia nigra. J. Neurochem. 68 6 (1997) 2458-2468
    • (1997) J. Neurochem. , vol.68 , Issue.6 , pp. 2458-2468
    • Venero, J.L.1    Revuelta, M.2    Cano, J.3    Machado, A.4
  • 107
    • 0033966487 scopus 로고    scopus 로고
    • Alpha-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP
    • Vila M., Vukosavic S., Jackson-Lewis V., Neystat M., Jakowec M., and Przedborski S. Alpha-synuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP. J. Neurochem. 74 2 (2000) 721-729
    • (2000) J. Neurochem. , vol.74 , Issue.2 , pp. 721-729
    • Vila, M.1    Vukosavic, S.2    Jackson-Lewis, V.3    Neystat, M.4    Jakowec, M.5    Przedborski, S.6
  • 109
    • 27444442414 scopus 로고    scopus 로고
    • Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60
    • Wadhwa R., Takano S., Kaur K., Aida S., Yaguchi T., Kaul Z., Hirano T., Taira K., and Kaul S.C. Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60. Biochem. J. 391 Pt 2 (2005) 185-190
    • (2005) Biochem. J. , vol.391 , Issue.PART 2 , pp. 185-190
    • Wadhwa, R.1    Takano, S.2    Kaur, K.3    Aida, S.4    Yaguchi, T.5    Kaul, Z.6    Hirano, T.7    Taira, K.8    Kaul, S.C.9
  • 111
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., and Yates III J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73 23 (2001) 5683-5690
    • (2001) Anal. Chem. , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 112
    • 14844297330 scopus 로고    scopus 로고
    • Intracellular retention of caveolin 1 in presenilin-deficient cells
    • Wood D.R., Nye J.S., Lamb N.J., Fernandez A., and Kitzmann M. Intracellular retention of caveolin 1 in presenilin-deficient cells. J. Biol. Chem. 280 8 (2005) 6663-6668
    • (2005) J. Biol. Chem. , vol.280 , Issue.8 , pp. 6663-6668
    • Wood, D.R.1    Nye, J.S.2    Lamb, N.J.3    Fernandez, A.4    Kitzmann, M.5
  • 113
    • 27144525246 scopus 로고    scopus 로고
    • Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation
    • Wu J.T., Lin H.C., Hu Y.C., and Chien C.T. Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation. Nat. Cell Biol. 7 10 (2005) 1014-1020
    • (2005) Nat. Cell Biol. , vol.7 , Issue.10 , pp. 1014-1020
    • Wu, J.T.1    Lin, H.C.2    Hu, Y.C.3    Chien, C.T.4
  • 114
    • 34948826976 scopus 로고    scopus 로고
    • Lifetime proteomic profiling of an A30P alpha-synuclein Drosophila model of Parkinson's disease
    • Xun Z., Sowell R.A., Kaufman T.C., and Clemmer D.E. Lifetime proteomic profiling of an A30P alpha-synuclein Drosophila model of Parkinson's disease. J. Proteome Res. 6 9 (2007) 3729-3738
    • (2007) J. Proteome Res. , vol.6 , Issue.9 , pp. 3729-3738
    • Xun, Z.1    Sowell, R.A.2    Kaufman, T.C.3    Clemmer, D.E.4
  • 115
    • 33846614962 scopus 로고    scopus 로고
    • Protein expression in a Drosophila model of Parkinson's disease
    • Xun Z., Sowell R.A., Kaufman T.C., and Clemmer D.E. Protein expression in a Drosophila model of Parkinson's disease. J. Proteome Res. 6 1 (2007) 348-357
    • (2007) J. Proteome Res. , vol.6 , Issue.1 , pp. 348-357
    • Xun, Z.1    Sowell, R.A.2    Kaufman, T.C.3    Clemmer, D.E.4
  • 116
    • 47849083301 scopus 로고    scopus 로고
    • Quantitative proteomics of a presymptomatic A53T a-synuclein drosophila model of Parkinson's disease
    • Xun Z., Sowell R.A., Kaufman T.C., and Clemmer D.E. Quantitative proteomics of a presymptomatic A53T a-synuclein drosophila model of Parkinson's disease. Mol. Cell Proteomics (2008)
    • (2008) Mol. Cell Proteomics
    • Xun, Z.1    Sowell, R.A.2    Kaufman, T.C.3    Clemmer, D.E.4
  • 117
    • 43449121006 scopus 로고    scopus 로고
    • Protein expression overlap: more important than which proteins change in expression?
    • Zabel C., Andreew A., Mao L., and Hartl D. Protein expression overlap: more important than which proteins change in expression?. Expert Rev. Proteomics 5 2 (2008) 187-205
    • (2008) Expert Rev. Proteomics , vol.5 , Issue.2 , pp. 187-205
    • Zabel, C.1    Andreew, A.2    Mao, L.3    Hartl, D.4
  • 119
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K., Huang H., Dawson V.L., and Dawson T.M. Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U.S.A. 97 24 (2000) 13354-13359
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.24 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6


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