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Volumn 4, Issue 2, 2007, Pages 227-238

Proteomics of Alzheimer's disease: Understanding mechanisms and seeking biomarkers

Author keywords

2D gel electrophoresis; Alzheimer's disease; Amyloid; Biomarker; Isobaric tag; Mass spectrometry; Plaque; Tangle; Tau

Indexed keywords

ALBUMIN; ALPHA 2 MACROGLOBULIN; APOLIPOPROTEIN A1; APOLIPOPROTEIN E; BETA 2 MICROGLOBULIN; BIOLOGICAL MARKER; CATHEPSIN D; CD5 ANTIGEN; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C4B; COMPLEMENT FACTOR H; CYSTATIN C; HEMOPEXIN; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; OROSOMUCOID; PREALBUMIN; RETINOL BINDING PROTEIN; TAU PROTEIN; TRYPSIN INHIBITOR;

EID: 34247101490     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.4.2.227     Document Type: Review
Times cited : (43)

References (121)
  • 1
    • 0035679752 scopus 로고    scopus 로고
    • Alzheimer's disease in the UK: Comparative evidence on cost of illness and volume of health services research funding
    • Lowin A, Knapp M, McCrone P. Alzheimer's disease in the UK: comparative evidence on cost of illness and volume of health services research funding. Int. J. Geriatr. Psychiatry 16, 1143-1148 (2001).
    • (2001) Int. J. Geriatr. Psychiatry , vol.16 , pp. 1143-1148
    • Lowin, A.1    Knapp, M.2    McCrone, P.3
  • 2
    • 13344269000 scopus 로고    scopus 로고
    • From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    • Wilkins MR, Pasquali C, Appel RD et al. From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Biotechnology (NY) 14, 61-65 (1996).
    • (1996) Biotechnology (NY) , vol.14 , pp. 61-65
    • Wilkins, M.R.1    Pasquali, C.2    Appel, R.D.3
  • 3
    • 0034852859 scopus 로고    scopus 로고
    • Mass spectrometry meets chip technology: A new proteomic tool in cancer research?
    • von Eggeling EF, Junker K, Fiedle W et al. Mass spectrometry meets chip technology: a new proteomic tool in cancer research? Electrophoresis 22, 2898-2902 (2001).
    • (2001) Electrophoresis , vol.22 , pp. 2898-2902
    • von Eggeling, E.F.1    Junker, K.2    Fiedle, W.3
  • 4
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi SP, Rist B, Gerber SA et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999 (1999).
    • (1999) Nat. Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3
  • 5
    • 0036708081 scopus 로고    scopus 로고
    • Proteomics goes quantitative: Measuring protein abundance
    • Steen H, Pandey A. Proteomics goes quantitative: measuring protein abundance. Trends Biotechnol. 20, 361-364 (2002).
    • (2002) Trends Biotechnol , vol.20 , pp. 361-364
    • Steen, H.1    Pandey, A.2
  • 6
    • 20444508181 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomics
    • Heck AJ, Krijgsveld J. Mass spectrometry-based quantitative proteomics. Expert. Rev. Proteomics 1, 317-326 (2004).
    • (2004) Expert. Rev. Proteomics , vol.1 , pp. 317-326
    • Heck, A.J.1    Krijgsveld, J.2
  • 7
    • 0346252168 scopus 로고    scopus 로고
    • Isolation of N-terminal protein sequence tags from cyanogen bromide cleaved proteins as a novel approach to investigate hydrophobic proteins
    • Kuhn K, Thompson A. Prinz T et al. Isolation of N-terminal protein sequence tags from cyanogen bromide cleaved proteins as a novel approach to investigate hydrophobic proteins. J. Proteome Res. 2, 598-609 (2003).
    • (2003) J. Proteome Res , vol.2 , pp. 598-609
    • Kuhn, K.1    Thompson, A.2    Prinz, T.3
  • 8
    • 33745249965 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson A, Schaefer J, Kuhn K et al. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 78, 4235 (2006).
    • (2006) Anal. Chem , vol.78 , pp. 4235
    • Thompson, A.1    Schaefer, J.2    Kuhn, K.3
  • 9
    • 0036669881 scopus 로고    scopus 로고
    • Amyloid-β oligomers: Their production, toxicity and therapeutic inhibition
    • Walsh DM, Klyubin I, Fadeeva JV et al. Amyloid-β oligomers: their production, toxicity and therapeutic inhibition. Biochem. Soc. Trans. 30, 552-557 (2002).
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 552-557
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 10
    • 29044443820 scopus 로고    scopus 로고
    • Physicochemical characteristics of soluble oligomeric Aβ and their pathologic role in Alzheimer's disease
    • Watson D, Castano E, Kokjohn TA et al. Physicochemical characteristics of soluble oligomeric Aβ and their pathologic role in Alzheimer's disease. Neurol. Res. 27, 869-881 (2005).
    • (2005) Neurol. Res , vol.27 , pp. 869-881
    • Watson, D.1    Castano, E.2    Kokjohn, T.A.3
  • 12
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid β protein in Alzheimer's disease
    • Mori H, Takio K, Ogawara M et al. Mass spectrometry of purified amyloid β protein in Alzheimer's disease. J. Biol. Chem. 267, 17082-17086 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3
  • 13
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • Miller DL, Papayannopoulos IA, Styles J et al. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch. Biochem. Biophys. 301, 41-52 (1993).
    • (1993) Arch. Biochem. Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3
  • 14
    • 12444337654 scopus 로고    scopus 로고
    • Truncated β-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach
    • Sergeant N, Bombois S, Ghestem A et al. Truncated β-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach. J. Neurochem. 85, 1581-1591 (2003).
    • (2003) J. Neurochem , vol.85 , pp. 1581-1591
    • Sergeant, N.1    Bombois, S.2    Ghestem, A.3
  • 15
    • 23844551164 scopus 로고    scopus 로고
    • Amino-terminally truncated Aβ peptide species are the main component of cotton wool plaques
    • Miravalle L, Calero M, Takao M et al. Amino-terminally truncated Aβ peptide species are the main component of cotton wool plaques. Biochemistry 44, 10810-10821 (2005).
    • (2005) Biochemistry , vol.44 , pp. 10810-10821
    • Miravalle, L.1    Calero, M.2    Takao, M.3
  • 16
    • 33750825049 scopus 로고    scopus 로고
    • High sensitivity analysis of amyloid-β peptide composition in amyloid deposits from human and PS2APP mouse brain
    • Guntert A, Dobeli H, Bohrmann B. High sensitivity analysis of amyloid-β peptide composition in amyloid deposits from human and PS2APP mouse brain. Neuroscience 143, 461-475 (2006).
    • (2006) Neuroscience , vol.143 , pp. 461-475
    • Guntert, A.1    Dobeli, H.2    Bohrmann, B.3
  • 17
    • 4344570364 scopus 로고    scopus 로고
    • Liao L, Cheng D, Wang J et al. Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J. Biol. Chem. 279(35), 37061-37068 (2004). •• Excellent example of a study combining advanced techniques (laser-capture microscopy and liquid chromatography tandem mass spectrometry). More evidence of axonal transport defects were demonstrated in Alzheimer's disease (AD) by showing dynein in the amyloid plaque.
    • Liao L, Cheng D, Wang J et al. Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J. Biol. Chem. 279(35), 37061-37068 (2004). •• Excellent example of a study combining advanced techniques (laser-capture microscopy and liquid chromatography tandem mass spectrometry). More evidence of axonal transport defects were demonstrated in Alzheimer's disease (AD) by showing dynein in the amyloid plaque.
  • 18
    • 33644855143 scopus 로고    scopus 로고
    • E and Alzheimer disease
    • Huang Y. Apolipoprotein E and Alzheimer disease. Neurology 66, S79-S85 (2006).
    • (2006) Neurology , vol.66
    • Apolipoprotein, H.Y.1
  • 19
    • 28444435458 scopus 로고    scopus 로고
    • Inflammation, the complement system and the diseases of aging
    • McGeer EG, Klegeris A, McGeer PL. Inflammation, the complement system and the diseases of aging. Neurobiol. Aging 26(Suppl. 1), 94-97 (2005).
    • (2005) Neurobiol. Aging , vol.26 , Issue.SUPPL. 1 , pp. 94-97
    • McGeer, E.G.1    Klegeris, A.2    McGeer, P.L.3
  • 21
    • 0035656206 scopus 로고    scopus 로고
    • Proteomic analysis of the brain in Alzheimer's disease: Molecular phenotype of a complex disease process
    • Schonberger SJ, Edgar PF, Kydd R et al. Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process. Proteomics 1, 1519-1528 (2001).
    • (2001) Proteomics , vol.1 , pp. 1519-1528
    • Schonberger, S.J.1    Edgar, P.F.2    Kydd, R.3
  • 22
    • 0035663035 scopus 로고    scopus 로고
    • Analysis of the proteomic profiling of brain tissue in Alzheimer's disease
    • Tsuji T, Shimohama S. Analysis of the proteomic profiling of brain tissue in Alzheimer's disease. Dis. Markers 17, 247-257 (2001).
    • (2001) Dis. Markers , vol.17 , pp. 247-257
    • Tsuji, T.1    Shimohama, S.2
  • 23
    • 0141767139 scopus 로고    scopus 로고
    • Proteomics in Alzheimer's disease: Insights into potential mechanisms of neurodegeneration
    • Butterfield DA, Boyd-Kimball D, Castegna A. Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration. J. Neurochem. 86, 1313-1327 (2003).
    • (2003) J. Neurochem , vol.86 , pp. 1313-1327
    • Butterfield, D.A.1    Boyd-Kimball, D.2    Castegna, A.3
  • 24
    • 0038472495 scopus 로고    scopus 로고
    • Proteomic identification of nitrated proteins in Alzheimer's disease brain
    • Castegna A, Thongboonkerd V, Klein JB et al. Proteomic identification of nitrated proteins in Alzheimer's disease brain. J. Neurochem. 85, 1394-1401 (2003).
    • (2003) J. Neurochem , vol.85 , pp. 1394-1401
    • Castegna, A.1    Thongboonkerd, V.2    Klein, J.B.3
  • 25
    • 4644352414 scopus 로고    scopus 로고
    • Proteomic approaches in brain research and neuropharmacology
    • Vercauteren FG, Bergeron JJ, Vandesande F et al. Proteomic approaches in brain research and neuropharmacology. Eur. J. Pharmacol. 500, 385-398 (2004).
    • (2004) Eur. J. Pharmacol , vol.500 , pp. 385-398
    • Vercauteren, F.G.1    Bergeron, J.J.2    Vandesande, F.3
  • 26
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • Gong CX, Liu F, Grundke-Iqbal I et al. Post-translational modifications of tau protein in Alzheimer's disease. J. Neural Transm. 112, 813-838 (2005).
    • (2005) J. Neural Transm , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3
  • 27
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E, Tung YC, Shaikh S et al. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24374-24384 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3
  • 28
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubuleassociated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M, Spillantini MG, Potier MC et al. Cloning and sequencing of the cDNA encoding an isoform of microtubuleassociated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 8, 393-399 (1989).
    • (1989) EMBO J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3
  • 29
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff WH, Johnson GV. Tau phosphorylation: physiological and pathological consequences. Biochim. Biophys. Acta 1739, 280-297 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 30
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin DT, Chait BT. Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 5, 591-602 (2001).
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 31
    • 0030218817 scopus 로고    scopus 로고
    • Selective detection and sequencing of phosphopeptides at the fentomole level by mass spectrometry
    • Carr SA, Huddleston MJ, Annan RS. Selective detection and sequencing of phosphopeptides at the fentomole level by mass spectrometry. Anal. Biochem. 239, 180-192 (1996).
    • (1996) Anal. Biochem , vol.239 , pp. 180-192
    • Carr, S.A.1    Huddleston, M.J.2    Annan, R.S.3
  • 32
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • Hanger DP, Betts JC, Loviny TL et al. New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J. Neurochem. 71, 2465-2476 (1998).
    • (1998) J. Neurochem , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3
  • 33
    • 0345096631 scopus 로고    scopus 로고
    • 2+/ calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry
    • 2+/ calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry. Neurosci. Lett. 353, 185-188 (2003).
    • (2003) Neurosci. Lett , vol.353 , pp. 185-188
    • Yoshimura, Y.1    Ichinose, T.2    Yamauchi, T.3
  • 34
    • 22244475384 scopus 로고    scopus 로고
    • Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase
    • Derkinderen P, Scales TM, Hanger DP et al. Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J. Neurosci. 25, 6584-6593 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 6584-6593
    • Derkinderen, P.1    Scales, T.M.2    Hanger, D.P.3
  • 35
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3β
    • Reynolds CH, Betts JC, Blackstock WP et al. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3β. J. Neurochem. 74, 1587-1595 (2000).
    • (2000) J. Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3
  • 36
    • 0035109902 scopus 로고    scopus 로고
    • Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry
    • Lund ET, McKenna R, Evans DB et al. Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry. J. Neurochem. 76, 1221-1232 (2001).
    • (2001) J. Neurochem , vol.76 , pp. 1221-1232
    • Lund, E.T.1    McKenna, R.2    Evans, D.B.3
  • 37
    • 0028807137 scopus 로고
    • Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation
    • Hensley K, Hall N, Subramaniam R et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J. Neurochem. 65, 2146-2156 (1995).
    • (1995) J. Neurochem , vol.65 , pp. 2146-2156
    • Hensley, K.1    Hall, N.2    Subramaniam, R.3
  • 38
    • 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
    • Boyd-Kimball D, Sultana R, Fai PH et al. Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid β-peptide (1-42) into rat brain: implications for Alzheimer's disease. Neuroscience 132, 313-324 (2005).
    • (2005) Neuroscience , vol.132 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Fai, P.H.3
  • 39
    • 33745990556 scopus 로고    scopus 로고
    • Boyd-Kimball D, Poon HF, Lynn BC et al. Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1-42): implications for Alzheimer's disease. Neurobiol. Aging 27(9), 1239-1249 (2005). • Using an experimental approach (in contrast to the observational studies that are the major focus of proteomics research in AD), this group shows convincingly that amyloid-β (Aβ) induces widespread protein oxidation in AD brain.
    • Boyd-Kimball D, Poon HF, Lynn BC et al. Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1-42): implications for Alzheimer's disease. Neurobiol. Aging 27(9), 1239-1249 (2005). • Using an experimental approach (in contrast to the observational studies that are the major focus of proteomics research in AD), this group shows convincingly that amyloid-β (Aβ) induces widespread protein oxidation in AD brain.
  • 40
    • 34247174565 scopus 로고    scopus 로고
    • Opii WO, Joshi G, Head E et al. Proteomic identification of brain proteins in the canine model of human aging following a long-term treatment with antioxidants and a program of behavioral enrichment: relevance to Alzheimer's disease. Neurobiol. Aging (2006) (Epub ahead of print). • Another paper from the same group, which uses proteomics to demonstrate oxidative changes induced by Aβ. Together, these two papers provide an elegant demonstration of the power of proteomics and the utility of animal models beyond the transgenic mouse in AD research.
    • Opii WO, Joshi G, Head E et al. Proteomic identification of brain proteins in the canine model of human aging following a long-term treatment with antioxidants and a program of behavioral enrichment: relevance to Alzheimer's disease. Neurobiol. Aging (2006) (Epub ahead of print). • Another paper from the same group, which uses proteomics to demonstrate oxidative changes induced by Aβ. Together, these two papers provide an elegant demonstration of the power of proteomics and the utility of animal models beyond the transgenic mouse in AD research.
  • 41
    • 2942659505 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain
    • Poon HF, Castegna A, Farr SA et al. Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain. Neuroscience 126, 915-926 (2004).
    • (2004) Neuroscience , vol.126 , pp. 915-926
    • Poon, H.F.1    Castegna, A.2    Farr, S.A.3
  • 42
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield DA, Boyd-Kimball D. The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim. Biophys. Acta 1703, 149-156 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 43
    • 0034834620 scopus 로고    scopus 로고
    • Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde
    • McGrath LT, McGleenon BM, Brennan S et al. Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde. QJM 94, 485-490 (2001).
    • (2001) QJM , vol.94 , pp. 485-490
    • McGrath, L.T.1    McGleenon, B.M.2    Brennan, S.3
  • 44
    • 0032905632 scopus 로고    scopus 로고
    • Protein-bound acrolein: A novel marker of oxidative stress in Alzheimer's disease
    • Calingasan NY, Uchida K, Gibson GE. Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease. J. Neurochem. 72, 751-756 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 751-756
    • Calingasan, N.Y.1    Uchida, K.2    Gibson, G.E.3
  • 45
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield DA, Perluigi M, Sultana R. Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur. J. Pharmacol. 545, 39-50 (2006).
    • (2006) Eur. J. Pharmacol , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 46
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine RL, Williams JA, Stadtman ER et al. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233, 346-357 (1994).
    • (1994) Methods Enzymol , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3
  • 47
    • 33645089917 scopus 로고    scopus 로고
    • Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach
    • Sultana R, Poon HF, Cai J et al. Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach. Neurobiol. Dis. 22, 76-87 (2006).
    • (2006) Neurobiol. Dis , vol.22 , pp. 76-87
    • Sultana, R.1    Poon, H.F.2    Cai, J.3
  • 48
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD
    • Sultana R, Boyd-Kimball D, Poon HF et al. Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neurobiol. Aging 27, 1564-1576 (2006).
    • (2006) Neurobiol. Aging , vol.27 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3
  • 49
    • 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 et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med. 33, 562-571 (2002).
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3
  • 50
    • 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
    • Lauderback CM, Hackett JM, Huang FF et al. 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. J. Neurochem. 78, 413-416 (2001).
    • (2001) J. Neurochem , vol.78 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3
  • 51
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease
    • Butterfield DA, Poon HF, St Clair CD et al. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol. Dis. 22, 223-232 (2006).
    • (2006) Neurobiol. Dis , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, C.D.3
  • 52
    • 0343775806 scopus 로고    scopus 로고
    • Plasma 24Shydroxycholesterol (cerebrosterol) is increased in Alzheimer and vascular demented patients
    • Lutjohann D, Papassotiropoulos A, Bjorkhem I et al. Plasma 24Shydroxycholesterol (cerebrosterol) is increased in Alzheimer and vascular demented patients. J. Lipid Res. 41, 195-198 (2000).
    • (2000) J. Lipid Res , vol.41 , pp. 195-198
    • Lutjohann, D.1    Papassotiropoulos, A.2    Bjorkhem, I.3
  • 53
    • 1542313783 scopus 로고    scopus 로고
    • Core biological marker candidates of Alzheimer's disease - perspectives for diagnosis, prediction of outcome and reflection of biological activity
    • Hampel H, Mitchell A, Blennow K et al. Core biological marker candidates of Alzheimer's disease - perspectives for diagnosis, prediction of outcome and reflection of biological activity. J. Neural Transm. 111, 247-272 (2004).
    • (2004) J. Neural Transm , vol.111 , pp. 247-272
    • Hampel, H.1    Mitchell, A.2    Blennow, K.3
  • 54
    • 33745959062 scopus 로고    scopus 로고
    • van OM, Hofman A, Soares HD et al. Plasma Aβ(1-40) and Aβ(1-42) and the risk of dementia: a prospective case-cohort study. Lancet Neurol. 5, 655-660 (2006). • Very large study demonstrating that Aβ can be accurately measured in plasma and that it is associated with risk of dementia. This raises the possibility of plasma-based, proteomics-derived markers of AD.
    • van OM, Hofman A, Soares HD et al. Plasma Aβ(1-40) and Aβ(1-42) and the risk of dementia: a prospective case-cohort study. Lancet Neurol. 5, 655-660 (2006). • Very large study demonstrating that Aβ can be accurately measured in plasma and that it is associated with risk of dementia. This raises the possibility of plasma-based, proteomics-derived markers of AD.
  • 55
    • 33645776682 scopus 로고    scopus 로고
    • Castano EM, Roher AE, Esh CL et al. Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects. Neurol. Res. 28, 155-163 (2006). •• Gel-based proteomics demonstrates widespread protein change in cerebrospinal fluid (CSF). Multiplexed biomarkers are the obvious conclusion from this work.
    • Castano EM, Roher AE, Esh CL et al. Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects. Neurol. Res. 28, 155-163 (2006). •• Gel-based proteomics demonstrates widespread protein change in cerebrospinal fluid (CSF). Multiplexed biomarkers are the obvious conclusion from this work.
  • 56
    • 33749120499 scopus 로고    scopus 로고
    • Proteomic analysis of cerebrospinal fluid changes related to postmortem interval
    • Finehout EJ, Franck Z, Relkin N et al. Proteomic analysis of cerebrospinal fluid changes related to postmortem interval. Clin. Chem. 52, 1906-1913 (2006).
    • (2006) Clin. Chem , vol.52 , pp. 1906-1913
    • Finehout, E.J.1    Franck, Z.2    Relkin, N.3
  • 57
    • 0036638618 scopus 로고    scopus 로고
    • Studies of potential cerebrospinal fluid molecular markers for Alzheimer's disease
    • Choe LH, Dutt MJ, Relkin N et al. Studies of potential cerebrospinal fluid molecular markers for Alzheimer's disease. Electrophoresis 23, 2247-2251 (2002).
    • (2002) Electrophoresis , vol.23 , pp. 2247-2251
    • Choe, L.H.1    Dutt, M.J.2    Relkin, N.3
  • 58
    • 0141957321 scopus 로고    scopus 로고
    • Proteomic studies of potential cerebrospinal fluid protein markers for Alzheimer's disease
    • Puchades M, Hansson SF, Nilsson CL et al. Proteomic studies of potential cerebrospinal fluid protein markers for Alzheimer's disease. Brain Res. Mol. Brain Res. 118, 140-146 (2003).
    • (2003) Brain Res. Mol. Brain Res , vol.118 , pp. 140-146
    • Puchades, M.1    Hansson, S.F.2    Nilsson, C.L.3
  • 59
    • 21044455621 scopus 로고    scopus 로고
    • Finehout EJ, Franck Z, Lee K.H. Complement protein isoforms in CSF as possible biomarkers for neurodegenerative disease. Dis. Markers 21, 93-101 (2005). • Another candidate-based protein study. This paper offers further evidence of a widespread change in complement activation in AD.
    • Finehout EJ, Franck Z, Lee K.H. Complement protein isoforms in CSF as possible biomarkers for neurodegenerative disease. Dis. Markers 21, 93-101 (2005). • Another candidate-based protein study. This paper offers further evidence of a widespread change in complement activation in AD.
  • 60
    • 0037117721 scopus 로고    scopus 로고
    • Proteome analysis of cerebrospinal fluid proteins in Alzheimer patients
    • Davidsson P, Westman-Brinkmalm A, Nilsson CL et al. Proteome analysis of cerebrospinal fluid proteins in Alzheimer patients. Neuroreport 13, 611-615 (2002).
    • (2002) Neuroreport , vol.13 , pp. 611-615
    • Davidsson, P.1    Westman-Brinkmalm, A.2    Nilsson, C.L.3
  • 61
    • 33847665648 scopus 로고    scopus 로고
    • Finehout EJ, Franck Z, Choe LH, Relkin N, Lee KH. Cerebrospinal fluid proteomic biomarkers for Alzheimer's disease. Ann. Neurol. 61, 120-129 (2007). •• See [69].
    • Finehout EJ, Franck Z, Choe LH, Relkin N, Lee KH. Cerebrospinal fluid proteomic biomarkers for Alzheimer's disease. Ann. Neurol. 61, 120-129 (2007). •• See [69].
  • 62
    • 0036424643 scopus 로고    scopus 로고
    • Identification of proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing as a prefractionation step followed by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation mass spectrometry
    • Davidsson P, Folkesson S, Christiansson M et al. Identification of proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing as a prefractionation step followed by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 16, 2083-2088 (2002).
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 2083-2088
    • Davidsson, P.1    Folkesson, S.2    Christiansson, M.3
  • 63
    • 0032589031 scopus 로고    scopus 로고
    • Identification of synaptic vesicle, pre- and postsynaptic proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing
    • Davidsson P, Puchades M, Blennow K. Identification of synaptic vesicle, pre- and postsynaptic proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing. Electrophoresis 20, 431-437 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 431-437
    • Davidsson, P.1    Puchades, M.2    Blennow, K.3
  • 64
    • 0032739315 scopus 로고    scopus 로고
    • A quantitative and immunohistochemical study on apolipoprotein E in grain tissue in Alzheimer's disease
    • Hesse C, Bogdanovic N, Davidsson P et al. A quantitative and immunohistochemical study on apolipoprotein E in grain tissue in Alzheimer's disease. Dementia 10, 452-459 (1999).
    • (1999) Dementia , vol.10 , pp. 452-459
    • Hesse, C.1    Bogdanovic, N.2    Davidsson, P.3
  • 65
    • 33745525307 scopus 로고    scopus 로고
    • Sheta EA, Appel SH, Goldknopf IL. 2D gel blood serum biomarkers reveal differential clinical proteomics of the neurodegenerative diseases. Expert. Rev. Proteomics 3, 45-62 (2006). •• Notes that blood-based biomarkers are feasible in AD. We agree with the conclusions that gel-based approaches have much to offer.
    • Sheta EA, Appel SH, Goldknopf IL. 2D gel blood serum biomarkers reveal differential clinical proteomics of the neurodegenerative diseases. Expert. Rev. Proteomics 3, 45-62 (2006). •• Notes that blood-based biomarkers are feasible in AD. We agree with the conclusions that gel-based approaches have much to offer.
  • 66
    • 23944475619 scopus 로고    scopus 로고
    • Differences among techniques for high-abundant protein depletion
    • Zolotarjova N, Martosella J, Nicol G et al. Differences among techniques for high-abundant protein depletion. Proteomics 5, 3304-3313 (2005).
    • (2005) Proteomics , vol.5 , pp. 3304-3313
    • Zolotarjova, N.1    Martosella, J.2    Nicol, G.3
  • 67
    • 25444515944 scopus 로고    scopus 로고
    • High-resolution serum proteomic profiling of Alzheimer disease samples reveals disease-specific, carrier-protein-bound mass signatures
    • Lopez MF, Mikulskis A, Kuzdzal S et al. High-resolution serum proteomic profiling of Alzheimer disease samples reveals disease-specific, carrier-protein-bound mass signatures. Clin. Chem. 51, 1946-1954 (2005).
    • (2005) Clin. Chem , vol.51 , pp. 1946-1954
    • Lopez, M.F.1    Mikulskis, A.2    Kuzdzal, S.3
  • 68
    • 0942276226 scopus 로고    scopus 로고
    • Mining biomarkers in human sera using proteomic tools
    • Zhang R, Barker L, Pinchev D et al. Mining biomarkers in human sera using proteomic tools. Proteomics 4, 244-256 (2004).
    • (2004) Proteomics , vol.4 , pp. 244-256
    • Zhang, R.1    Barker, L.2    Pinchev, D.3
  • 69
    • 33750596715 scopus 로고    scopus 로고
    • Hye A, Lynham S, Thambisetty M et al. Proteome-based plasma biomarkers for Alzheimer's disease. Brain 129, 3042-3050 (2006). •• Our study and Finehout et al [61] both use proteomics combined with multivariate analyses to identify putative markers of AD. These are important papers showing the potential of proteomic approaches in both plasma and CSF. Both fluids may be productive sources of biomarkers: CSF, as a sample fluid closer to disease, is likely to show a greater signal (as suggested by a comparison of the data from these two papers). Plasma, as a sample fluid that is easier to access, would be easier to use in the clinical setting. Both approaches are likely to be pursued vigorously to find the best combination of specificity and utility.
    • Hye A, Lynham S, Thambisetty M et al. Proteome-based plasma biomarkers for Alzheimer's disease. Brain 129, 3042-3050 (2006). •• Our study and Finehout et al [61] both use proteomics combined with multivariate analyses to identify putative markers of AD. These are important papers showing the potential of proteomic approaches in both plasma and CSF. Both fluids may be productive sources of biomarkers: CSF, as a sample fluid closer to disease, is likely to show a greater signal (as suggested by a comparison of the data from these two papers). Plasma, as a sample fluid that is easier to access, would be easier to use in the clinical setting. Both approaches are likely to be pursued vigorously to find the best combination of specificity and utility.
  • 70
    • 32044446447 scopus 로고    scopus 로고
    • Proteomic identification of lower apolipoprotein A-I in Alzheimer's disease
    • Liu HC, Hu CJ, Chang JG et al. Proteomic identification of lower apolipoprotein A-I in Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 21, 155-161 (2006).
    • (2006) Dement. Geriatr. Cogn. Disord , vol.21 , pp. 155-161
    • Liu, H.C.1    Hu, C.J.2    Chang, J.G.3
  • 71
    • 0041358773 scopus 로고    scopus 로고
    • Carrette O, Demalte I, Scherl A et al. A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease. Proteomics 3, 1486-1494 (2003). • Although a small study, this early demonstration that surface-enhanced laser desorption/ionization analysis of CSF can be used as a potential diagnostic marker for AD was important.
    • Carrette O, Demalte I, Scherl A et al. A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease. Proteomics 3, 1486-1494 (2003). • Although a small study, this early demonstration that surface-enhanced laser desorption/ionization analysis of CSF can be used as a potential diagnostic marker for AD was important.
  • 72
    • 1542722311 scopus 로고    scopus 로고
    • Amyloid β peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: Evidence of novel biomarkers in Alzheimer's disease
    • Lewczuk P, Esselmann H, Groemer TW et al. Amyloid β peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: evidence of novel biomarkers in Alzheimer's disease. Biol. Psychiatry 55, 524-530 (2004).
    • (2004) Biol. Psychiatry , vol.55 , pp. 524-530
    • Lewczuk, P.1    Esselmann, H.2    Groemer, T.W.3
  • 73
    • 9244240337 scopus 로고    scopus 로고
    • Maddalena AS, Papassotiropoulos A, Gonzalez-Agosti C et al. Cerebrospinal fluid profile of amyloid β peptides in patients with Alzheimer's disease determined by protein biochip technology. Neurodegener. Dis. 1, 231-235 (2004). •• Rather than attempting to profile the proteome, these authors have profiled the range of amyloid peptides in CSF. This is important both for the understanding of the metabolism of amyloid precursor protein and as a potential biomarker that is potentially more specific than Aβ42.
    • Maddalena AS, Papassotiropoulos A, Gonzalez-Agosti C et al. Cerebrospinal fluid profile of amyloid β peptides in patients with Alzheimer's disease determined by protein biochip technology. Neurodegener. Dis. 1, 231-235 (2004). •• Rather than attempting to profile the proteome, these authors have profiled the range of amyloid peptides in CSF. This is important both for the understanding of the metabolism of amyloid precursor protein and as a potential biomarker that is potentially more specific than Aβ42.
  • 74
    • 20944443414 scopus 로고    scopus 로고
    • Quantitative proteomics of cerebrospinal fluid from patients with Alzheimer disease
    • Zhang J, Goodlett DR, Quinn JF et al. Quantitative proteomics of cerebrospinal fluid from patients with Alzheimer disease. J. Alzheimers Dis. 7, 125-133 (2005).
    • (2005) J. Alzheimers Dis , vol.7 , pp. 125-133
    • Zhang, J.1    Goodlett, D.R.2    Quinn, J.F.3
  • 75
    • 33747409456 scopus 로고    scopus 로고
    • Abdi F, Quinn JF, Jankovic J et al. Detection of biomarkers with a multiplex quantitative proteomic platform in cerebrospinal fluid of patients with neurodegenerative disorders. J. Alzheimers Dis. 9, 293-348 (2006). •• One of the first studies to use multiplexed mass spectrometry-based approaches for biomarker discovery. This is an impressive paper and perhaps a sign of future developments in proteomics of AD.
    • Abdi F, Quinn JF, Jankovic J et al. Detection of biomarkers with a multiplex quantitative proteomic platform in cerebrospinal fluid of patients with neurodegenerative disorders. J. Alzheimers Dis. 9, 293-348 (2006). •• One of the first studies to use multiplexed mass spectrometry-based approaches for biomarker discovery. This is an impressive paper and perhaps a sign of future developments in proteomics of AD.
  • 76
    • 0038417096 scopus 로고    scopus 로고
    • Veerhuis R, Van Breemen MJ, Hoozemans JM et al. Amyloid β plaque-associated proteins C1q and SAP enhance the Aβ1-42 peptide-induced cytokine secretion by adult human microglia in vitro. Acta Neuropathol. (Berl.) 105(2), 135-144 (2003).
    • Veerhuis R, Van Breemen MJ, Hoozemans JM et al. Amyloid β plaque-associated proteins C1q and SAP enhance the Aβ1-42 peptide-induced cytokine secretion by adult human microglia in vitro. Acta Neuropathol. (Berl.) 105(2), 135-144 (2003).
  • 77
    • 0028787769 scopus 로고
    • Distribution of β amyloid associated proteins in plaques in Alzheimer's disease and in the non-demented elderly
    • Zhan SS, Veerhuis R, Kamphorst W, Eikelenboom P. Distribution of β amyloid associated proteins in plaques in Alzheimer's disease and in the non-demented elderly. Neurodegeneration 4(3), 291-297 (1995).
    • (1995) Neurodegeneration , vol.4 , Issue.3 , pp. 291-297
    • Zhan, S.S.1    Veerhuis, R.2    Kamphorst, W.3    Eikelenboom, P.4
  • 78
    • 0032487575 scopus 로고    scopus 로고
    • Prominent expression of presenilin-1 in senile plaques and reactive astrocytes in Alzheimer's disease brain
    • Weggen S, Diehlmann A, Buslei R, Beyreuther K, Bayer TA. Prominent expression of presenilin-1 in senile plaques and reactive astrocytes in Alzheimer's disease brain. Neuroreport 9(14), 3279-3283 (1998).
    • (1998) Neuroreport , vol.9 , Issue.14 , pp. 3279-3283
    • Weggen, S.1    Diehlmann, A.2    Buslei, R.3    Beyreuther, K.4    Bayer, T.A.5
  • 79
    • 0030025635 scopus 로고    scopus 로고
    • Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease
    • Masliah E, Iwai A, Mallory M, Ueda K, Saitoh T. Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease. Am. J. Pathol. 148(1), 201-210 (1996).
    • (1996) Am. J. Pathol , vol.148 , Issue.1 , pp. 201-210
    • Masliah, E.1    Iwai, A.2    Mallory, M.3    Ueda, K.4    Saitoh, T.5
  • 80
    • 0035141524 scopus 로고    scopus 로고
    • Prion protein expression in senile plaques in Alzheimer's disease
    • Ferrer I, Blanco R, Carmona M et al. Prion protein expression in senile plaques in Alzheimer's disease. Acta Neuropathol. (Berl.) 101(1), 49-56 (2001).
    • (2001) Acta Neuropathol. (Berl.) , vol.101 , Issue.1 , pp. 49-56
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3
  • 81
    • 0025971426 scopus 로고
    • Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease
    • Namba Y, Tomonaga M, Kawasaki H, Otomo E, Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 541(1), 163-166 (1991).
    • (1991) Brain Res , vol.541 , Issue.1 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomo, E.4    Ikeda, K.5
  • 82
    • 0042360512 scopus 로고    scopus 로고
    • Analysis of glial acidic fibrillary protein in the human entorhinal cortex during aging and in Alzheimer's disease
    • Porchet R, Probst A, Bouras C, Draberova E, Draber P, Riederer BM. Analysis of glial acidic fibrillary protein in the human entorhinal cortex during aging and in Alzheimer's disease. Proteomics 3(8), 1476-1485 (2003).
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1476-1485
    • Porchet, R.1    Probst, A.2    Bouras, C.3    Draberova, E.4    Draber, P.5    Riederer, B.M.6
  • 83
    • 0028926976 scopus 로고
    • Interleukin-1 expression in different plaque types in Alzheimer's disease, significance in plaque evolution
    • Griffin WS, Sheng JG, Roberts GW, Mrak RE. Interleukin-1 expression in different plaque types in Alzheimer's disease, significance in plaque evolution. J. Neuropathol. Exp. Neurol. 54(2), 276-281 (1995).
    • (1995) J. Neuropathol. Exp. Neurol , vol.54 , Issue.2 , pp. 276-281
    • Griffin, W.S.1    Sheng, J.G.2    Roberts, G.W.3    Mrak, R.E.4
  • 84
    • 0029986869 scopus 로고    scopus 로고
    • Occurrence of interleukin-6 in cortical plaques of Alzheimer's disease patients may precede transformation of diffuse into neuritic plaques
    • Hull M, Berger M, Volk B, Bauer J. Occurrence of interleukin-6 in cortical plaques of Alzheimer's disease patients may precede transformation of diffuse into neuritic plaques. Ann. NY Acad. Sci. 777, 205-212 (1996).
    • (1996) Ann. NY Acad. Sci , vol.777 , pp. 205-212
    • Hull, M.1    Berger, M.2    Volk, B.3    Bauer, J.4
  • 85
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • Perry G, Friedman R, Shaw G, Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc. Natl Acad. Sci. USA 84(9), 3033-3036 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , Issue.9 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 86
    • 0033605607 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in the Alzheimer's disease brain prominent localization in neurons and senile plaques
    • Bernstein HG, Ansorge S, Riederer P, Reiser M, Frolich L, Bogerts B. Insulin-degrading enzyme in the Alzheimer's disease brain prominent localization in neurons and senile plaques. Neurosci. Lett. 263(2-3), 161-164 (1999).
    • (1999) Neurosci. Lett , vol.263 , Issue.2-3 , pp. 161-164
    • Bernstein, H.G.1    Ansorge, S.2    Riederer, P.3    Reiser, M.4    Frolich, L.5    Bogerts, B.6
  • 88
    • 0026601404 scopus 로고
    • α1-antitrypsin and α1-antichymotrypsin are in the lesions of Alzheimer's disease
    • Gollin PA, Kalaria RN, Eikelenboom P, Rozemuller A, Perry G. α1-antitrypsin and α1-antichymotrypsin are in the lesions of Alzheimer's disease. Neuroreport 3(2), 201-203 (1992).
    • (1992) Neuroreport , vol.3 , Issue.2 , pp. 201-203
    • Gollin, P.A.1    Kalaria, R.N.2    Eikelenboom, P.3    Rozemuller, A.4    Perry, G.5
  • 89
    • 0024819090 scopus 로고
    • Immunodetection of cathepsin D in neuritic plaques found in brains of patients with dementia of Alzheimer type
    • Bernstein HG, Bruszis S, Schmidt D, Wiederanders B, Dorn A. Immunodetection of cathepsin D in neuritic plaques found in brains of patients with dementia of Alzheimer type. J. Hirnforsch 30(5), 613-618 (1989).
    • (1989) J. Hirnforsch , vol.30 , Issue.5 , pp. 613-618
    • Bernstein, H.G.1    Bruszis, S.2    Schmidt, D.3    Wiederanders, B.4    Dorn, A.5
  • 90
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 165(2), 523-531 (2004).
    • (2004) Am. J. Pathol , vol.165 , Issue.2 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    LeBlanc, A.C.6
  • 91
    • 14744281153 scopus 로고    scopus 로고
    • Quantification of the Aβ peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry
    • Rufenacht P, Guntert A, Bohrmann B, Ducret A, Dobeli H. Quantification of the Aβ peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry. J. Mass Spectrom. 40(2), 193-201 (2005).
    • (2005) J. Mass Spectrom , vol.40 , Issue.2 , pp. 193-201
    • Rufenacht, P.1    Guntert, A.2    Bohrmann, B.3    Ducret, A.4    Dobeli, H.5
  • 92
    • 0026058252 scopus 로고
    • Synaptophysin and chromogranin A immunoreactivities in senile plaques of Alzheimer's disease
    • Brion JP, Couck AM, Bruce M, Anderton B, Flament-Durand J. Synaptophysin and chromogranin A immunoreactivities in senile plaques of Alzheimer's disease. Brain Res. 539(1), 143-150 (1991).
    • (1991) Brain Res , vol.539 , Issue.1 , pp. 143-150
    • Brion, J.P.1    Couck, A.M.2    Bruce, M.3    Anderton, B.4    Flament-Durand, J.5
  • 93
    • 0037224717 scopus 로고    scopus 로고
    • Neuregulin-1 and erbB4 immunoreactivity is associated with neuritic plaques in Alzheimer disease brain and in a transgenic model of Alzheimer disease
    • Chaudhury AR, Gerecke KM, Wyss JM, Morgan DG, Gordon MN, Carroll SL. Neuregulin-1 and erbB4 immunoreactivity is associated with neuritic plaques in Alzheimer disease brain and in a transgenic model of Alzheimer disease. J. Neuropathol. Exp. Neurol. 62(1), 42-54 (2003).
    • (2003) J. Neuropathol. Exp. Neurol , vol.62 , Issue.1 , pp. 42-54
    • Chaudhury, A.R.1    Gerecke, K.M.2    Wyss, J.M.3    Morgan, D.G.4    Gordon, M.N.5    Carroll, S.L.6
  • 95
    • 33745107526 scopus 로고    scopus 로고
    • Tomoregulin-2 is found extensively in plaques in Alzheimer's disease brain
    • Siegel DA, Davies P, Dobrenis K, Huang M. Tomoregulin-2 is found extensively in plaques in Alzheimer's disease brain. J. Neurochem. 98(1), 34-44 (2006).
    • (2006) J. Neurochem , vol.98 , Issue.1 , pp. 34-44
    • Siegel, D.A.1    Davies, P.2    Dobrenis, K.3    Huang, M.4
  • 96
    • 0028044613 scopus 로고
    • Involvement of clathrin light chains in the pathology of Alzheimer's disease
    • Nakamura Y, Takeda M, Yoshimi K et al. Involvement of clathrin light chains in the pathology of Alzheimer's disease. Acta Neuropathol. (Berl.) 87(1), 23-31 (1994).
    • (1994) Acta Neuropathol. (Berl.) , vol.87 , Issue.1 , pp. 23-31
    • Nakamura, Y.1    Takeda, M.2    Yoshimi, K.3
  • 97
    • 1542327619 scopus 로고    scopus 로고
    • Induction of brain-derived neurotrophic factor in plaque-associated glial cells of aged APP23 transgenic mice
    • Burbach GJ, Hellweg R, Haas CA et al. Induction of brain-derived neurotrophic factor in plaque-associated glial cells of aged APP23 transgenic mice. J. Neurosci. 24(10), 2421-2430 (2004).
    • (2004) J. Neurosci , vol.24 , Issue.10 , pp. 2421-2430
    • Burbach, G.J.1    Hellweg, R.2    Haas, C.A.3
  • 98
    • 0032517789 scopus 로고    scopus 로고
    • Fibroblast growth factor (FGF)-9 immunoreactivity in senile plaques
    • Nakamura S, Arima K, Haga S et al. Fibroblast growth factor (FGF)-9 immunoreactivity in senile plaques. Brain Res. 814(1-2), 222-225 (1998).
    • (1998) Brain Res , vol.814 , Issue.1-2 , pp. 222-225
    • Nakamura, S.1    Arima, K.2    Haga, S.3
  • 99
    • 0027450057 scopus 로고
    • Transforming growth factor-β1 is in plaques in Alzheimer and Down pathologies
    • van der Wal EA, Gomez-Pinilla F, Cotman CW. Transforming growth factor-β1 is in plaques in Alzheimer and Down pathologies. Neuroreport 4(1), 69-72 (1993).
    • (1993) Neuroreport , vol.4 , Issue.1 , pp. 69-72
    • van der Wal, E.A.1    Gomez-Pinilla, F.2    Cotman, C.W.3
  • 101
    • 0023736761 scopus 로고
    • Immunoreactive epidermal growth factor receptors in neuritic plaques from patients with Alzheimer's disease
    • Birecree E, Whetsell WO Jr, Stoscheck C, King LE Jr, Nanney LB. Immunoreactive epidermal growth factor receptors in neuritic plaques from patients with Alzheimer's disease. J. Neuropathol. Exp. Neurol. 47(5), 549-560 (1988).
    • (1988) J. Neuropathol. Exp. Neurol , vol.47 , Issue.5 , pp. 549-560
    • Birecree, E.1    Whetsell Jr, W.O.2    Stoscheck, C.3    King Jr, L.E.4    Nanney, L.B.5
  • 102
    • 0021988724 scopus 로고
    • Somatostatin immunoreactivity in neuritic plaques of Alzheimer's patients
    • Morrison JH, Rogers J, Scherr S, Benoit R, Bloom FE. Somatostatin immunoreactivity in neuritic plaques of Alzheimer's patients. Nature 314(6006), 90-92 (1985).
    • (1985) Nature , vol.314 , Issue.6006 , pp. 90-92
    • Morrison, J.H.1    Rogers, J.2    Scherr, S.3    Benoit, R.4    Bloom, F.E.5
  • 104
    • 17644397044 scopus 로고    scopus 로고
    • Histological co-localization of iron in Aβ plaques of PS/APP transgenic mice
    • Falangola MF, Lee SP, Nixon RA, Duff K, Helpern JA. Histological co-localization of iron in Aβ plaques of PS/APP transgenic mice. Neurochem. Res. 30(2), 201-205 (2005).
    • (2005) Neurochem. Res , vol.30 , Issue.2 , pp. 201-205
    • Falangola, M.F.1    Lee, S.P.2    Nixon, R.A.3    Duff, K.4    Helpern, J.A.5
  • 105
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • Suh SW, Jensen KB, Jensen MS et al. Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res. 852(2), 274-278 (2000).
    • (2000) Brain Res , vol.852 , Issue.2 , pp. 274-278
    • Suh, S.W.1    Jensen, K.B.2    Jensen, M.S.3
  • 107
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the β-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome
    • Snow AD, Mar H, Nochlin D et al. Early accumulation of heparan sulfate in neurons and in the β-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome. Am. J. Pathol. 137(5), 1253-1270 (1990).
    • (1990) Am. J. Pathol , vol.137 , Issue.5 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3
  • 108
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow AD, Mar H, Nochlin D, Kresse H, Wight TN. Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease. J. Histochem. Cytochem. 40(1), 105-113 (1992).
    • (1992) J. Histochem. Cytochem , vol.40 , Issue.1 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 109
    • 0036793927 scopus 로고    scopus 로고
    • Collagen XVIII, a novel heparan sulfate proteoglycan associated with vascular amyloid depositions and senile plaques in Alzheimer's disease brains
    • van Horssen HJ, Wilhelmus MM, Heljasvaara R et al. Collagen XVIII, a novel heparan sulfate proteoglycan associated with vascular amyloid depositions and senile plaques in Alzheimer's disease brains. Brain Pathol. 12(4), 456-462 (2002).
    • (2002) Brain Pathol , vol.12 , Issue.4 , pp. 456-462
    • van Horssen, H.J.1    Wilhelmus, M.M.2    Heljasvaara, R.3
  • 110
    • 0037474140 scopus 로고    scopus 로고
    • Co-localization of cholesterol, apolipoprotein E and fibrillar Aβ in amyloid plaques
    • Burns MP, Noble WJ, Olm V et al. Co-localization of cholesterol, apolipoprotein E and fibrillar Aβ in amyloid plaques. Brain Res. Mol. Brain Res. 110(1), 119-125 (2003).
    • (2003) Brain Res. Mol. Brain Res , vol.110 , Issue.1 , pp. 119-125
    • Burns, M.P.1    Noble, W.J.2    Olm, V.3
  • 111
    • 0032707107 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase immunoreactivity in the Alzheimer disease hippocampus, association with Hirano bodies, neurofibrillary tangles, and senile plaques
    • Lee SC, Zhao ML, Hirano A, Dickson DW. Inducible nitric oxide synthase immunoreactivity in the Alzheimer disease hippocampus, association with Hirano bodies, neurofibrillary tangles, and senile plaques. J. Neuropathol. Exp. Neurol. 58(11), 1163-1169 (1999).
    • (1999) J. Neuropathol. Exp. Neurol , vol.58 , Issue.11 , pp. 1163-1169
    • Lee, S.C.1    Zhao, M.L.2    Hirano, A.3    Dickson, D.W.4
  • 112
    • 0031596151 scopus 로고    scopus 로고
    • NF-κB immunoreactivity is observed in association with β A4 diffuse plaques in patients with Alzheimer's disease
    • Ferrer I, Marti E, Lopez E, Tortosa A. NF-κB immunoreactivity is observed in association with β A4 diffuse plaques in patients with Alzheimer's disease. Neuropathol. Appl. Neurobiol. 24(4), 271-277 (1998).
    • (1998) Neuropathol. Appl. Neurobiol , vol.24 , Issue.4 , pp. 271-277
    • Ferrer, I.1    Marti, E.2    Lopez, E.3    Tortosa, A.4
  • 114
    • 0033614713 scopus 로고    scopus 로고
    • Bleomycin hydrolase immunoreactivity in senile plaque in the brains of patients with Alzheimer's disease
    • Namba Y, Ouchi Y, Takeda A, Ueki A, Ikeda K. Bleomycin hydrolase immunoreactivity in senile plaque in the brains of patients with Alzheimer's disease. Brain Res. 830(1), 200-202 (1999).
    • (1999) Brain Res , vol.830 , Issue.1 , pp. 200-202
    • Namba, Y.1    Ouchi, Y.2    Takeda, A.3    Ueki, A.4    Ikeda, K.5
  • 115
    • 0035966144 scopus 로고    scopus 로고
    • Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice
    • Wirths O, Multhaup G, Czech C et al. Reelin in plaques of β-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci. Lett. 316(3), 145-148 (2001).
    • (2001) Neurosci. Lett , vol.316 , Issue.3 , pp. 145-148
    • Wirths, O.1    Multhaup, G.2    Czech, C.3
  • 116
    • 0037147688 scopus 로고    scopus 로고
    • Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin α
    • Reiser G, Bernstein HG. Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin α. Neuroreport 13(18), 2417-2419 (2002).
    • (2002) Neuroreport , vol.13 , Issue.18 , pp. 2417-2419
    • Reiser, G.1    Bernstein, H.G.2
  • 117
    • 0027131813 scopus 로고
    • Immunoreactivity of the nuclear antigen p105 is associated with plaques and tangles in Alzheimer's disease
    • Masliah E, Mallory M, Alford M, Hansen LA, Saitoh T. Immunoreactivity of the nuclear antigen p105 is associated with plaques and tangles in Alzheimer's disease. Lab. Invest. 69(5), 562-569 (1993).
    • (1993) Lab. Invest , vol.69 , Issue.5 , pp. 562-569
    • Masliah, E.1    Mallory, M.2    Alford, M.3    Hansen, L.A.4    Saitoh, T.5
  • 118
    • 0026601368 scopus 로고
    • Apolipoprotein B immunoreactivity in senile plaque and vascular amyloids and neurofibrillary tangles in the brains of patients with Alzheimer's disease
    • Namba Y, Tsuchiya H, Ikeda K. Apolipoprotein B immunoreactivity in senile plaque and vascular amyloids and neurofibrillary tangles in the brains of patients with Alzheimer's disease. Neurosci. Lett. 134(2), 264-266 (1992).
    • (1992) Neurosci. Lett , vol.134 , Issue.2 , pp. 264-266
    • Namba, Y.1    Tsuchiya, H.2    Ikeda, K.3
  • 119
    • 26944432332 scopus 로고    scopus 로고
    • Apolipoprotein D is a component of compact but not diffuse amyloid-β plaques in Alzheimer's disease temporal cortex
    • Desai PP, Ikonomovic MD, Abrahamson EE et al. Apolipoprotein D is a component of compact but not diffuse amyloid-β plaques in Alzheimer's disease temporal cortex. Neurobiol. Dis. 20(2), 574-582 (2005).
    • (2005) Neurobiol. Dis , vol.20 , Issue.2 , pp. 574-582
    • Desai, P.P.1    Ikonomovic, M.D.2    Abrahamson, E.E.3
  • 120
    • 21744452500 scopus 로고    scopus 로고
    • Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in Alzheimer's disease brain
    • Martin-Rehrmann MD, Hoe HS, Capuani EM, Rebeck GW. Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in Alzheimer's disease brain. Neurotox Res. 7(3), 231-242 (2005).
    • (2005) Neurotox Res , vol.7 , Issue.3 , pp. 231-242
    • Martin-Rehrmann, M.D.1    Hoe, H.S.2    Capuani, E.M.3    Rebeck, G.W.4
  • 121
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: Protein profiling and biomarker identification
    • Issaq HJ, Veenstra TD, Conrads TP, Felschow D. The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem. Biophys. Res. Commun. 293(3), 587-592 (2002).
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , Issue.3 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4


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