메뉴 건너뛰기




Volumn 13, Issue 4, 2014, Pages 2056-2068

Quantification of the brain proteome in Alzheimer's disease using multiplexed mass spectrometry

Author keywords

Alzheimer's disease (AD); brain tissue; dimethyl labeling (DML); mass spectrometry (MS); quantitative proteomics

Indexed keywords

ACETYL COENZYME A ACETYLTRANSFERASE; APOLIPOPROTEIN D; BRAIN PROTEIN; CALPHOBINDIN II; CARBONATE DEHYDRATASE II; CATHEPSIN D; CLATHRIN HEAVY CHAIN; CLATHRIN HEAVY CHAIN 1; COFILIN 1; CYTOCHROME C; DIHYDROPTERIDINE REDUCTASE; GLIAL FIBRILLARY ACIDIC PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE; LIPOCORTIN 5; MALATE DEHYDROGENASE; NEUROTRIMIN; OXIDOREDUCTASE; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PEROXIREDOXIN 6; SEPTIN; SEPTIN 2; SEPTIN 3; SEPTIN 5; SERUM ALBUMIN; STABLE ISOTOPE; SYNAPSIN I; SYNDAPIN 1; SYNTAXIN 1A; TRANSKETOLASE; UNCLASSIFIED DRUG; NERVE PROTEIN; PROTEOME;

EID: 84898767050     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr401202d     Document Type: Article
Times cited : (85)

References (90)
  • 2
    • 0014851803 scopus 로고
    • Observations on brains of demented old people
    • Tomlinso, Be; Blessed, G.; Roth, M. Observations on brains of demented old people J. Neurol. Sci. 1970, 11 (3) 205-&
    • (1970) J. Neurol. Sci. , vol.11 , Issue.3 , pp. 205
    • Tomlinso, B.1    Blessed, G.2    Roth, M.3
  • 3
    • 0026597063 scopus 로고
    • Alzheimers disease - The amyloid cascade hypothesis
    • Hardy, J. A.; Higgins, G. A. Alzheimers disease-the amyloid cascade hypothesis Science 1992, 256 (5054) 184-185
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 4
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis
    • Swerdlow, R. H.; Burns, J. M.; Khan, S. M. The Alzheimer's disease mitochondrial cascade hypothesis J. Alzheimers Dis. 2010, 20, S265-S279
    • (2010) J. Alzheimers Dis. , vol.20
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 6
    • 0029609264 scopus 로고
    • Tau protein in cerebrospinal fluid - A biochemical marker for axonal degeneration in Alzheimer disease?
    • Blennow, K.; Wallin, A.; Agren, H.; Spenger, C.; Siegfried, J.; Vanmechelen, E. tau protein in cerebrospinal fluid-A biochemical marker for axonal degeneration in Alzheimer disease? Mol. Chem. Neuropathol. 1995, 26 (3) 231-245
    • (1995) Mol. Chem. Neuropathol. , vol.26 , Issue.3 , pp. 231-245
    • Blennow, K.1    Wallin, A.2    Agren, H.3    Spenger, C.4    Siegfried, J.5    Vanmechelen, E.6
  • 8
    • 0030801045 scopus 로고    scopus 로고
    • Cerebrospinal fluid apolipoprotein e (apoE) levels in Alzheimer's disease patients are increased at follow up and show a correlation with levels of tau protein
    • Lindh, M.; Blomberg, M.; Jensen, M.; Basun, H.; Lannfelt, L.; Engvall, B.; Scharnagel, H.; Marz, W.; Wahlund, L. O.; Cowburn, R. F. Cerebrospinal fluid apolipoprotein E (apoE) levels in Alzheimer's disease patients are increased at follow up and show a correlation with levels of tau protein Neurosci. Lett. 1997, 229 (2) 85-88
    • (1997) Neurosci. Lett. , vol.229 , Issue.2 , pp. 85-88
    • Lindh, M.1    Blomberg, M.2    Jensen, M.3    Basun, H.4    Lannfelt, L.5    Engvall, B.6    Scharnagel, H.7    Marz, W.8    Wahlund, L.O.9    Cowburn, R.F.10
  • 12
    • 0029175962 scopus 로고
    • 2-Dimensional analysis of qualitative and quantitative changes in blood-cell proteins in Alzheimers-disease - Search for extraneuronal markers
    • Mattila, K. M.; Frey, H. 2-Dimensional analysis of qualitative and quantitative changes in blood-cell proteins in Alzheimers-disease-search for extraneuronal markers Appl. Theor. Electrophor. 1995, 4 (4) 189-196
    • (1995) Appl. Theor. Electrophor. , vol.4 , Issue.4 , pp. 189-196
    • Mattila, K.M.1    Frey, H.2
  • 14
    • 79955663597 scopus 로고    scopus 로고
    • Systems biology of Alzheimer's disease: How diverse molecular changes result in memory impairment in AD
    • Juhasz, G.; Foldi, I.; Penke, B. Systems biology of Alzheimer's disease: How diverse molecular changes result in memory impairment in AD Neurochem. Int. 2011, 58 (7) 739-750
    • (2011) Neurochem. Int. , vol.58 , Issue.7 , pp. 739-750
    • Juhasz, G.1    Foldi, I.2    Penke, B.3
  • 15
    • 57749184790 scopus 로고    scopus 로고
    • Proteomics in animal models of Alzheimer's and Parkinson's diseases
    • Sowell, R. A.; Owen, J. B.; Butterfield, D. A. Proteomics in animal models of Alzheimer's and Parkinson's diseases Ageing Res. Rev. 2009, 8 (1) 1-17
    • (2009) Ageing Res. Rev. , vol.8 , Issue.1 , pp. 1-17
    • Sowell, R.A.1    Owen, J.B.2    Butterfield, D.A.3
  • 16
    • 77249179997 scopus 로고    scopus 로고
    • An update on clinical proteomics in Alzheimer's research
    • Korolainen, M. A.; Nyman, T. A.; Aittokallio, T.; Pirttila, T. An update on clinical proteomics in Alzheimer's research J. Neurochem. 2010, 112 (6) 1386-1414
    • (2010) J. Neurochem. , vol.112 , Issue.6 , pp. 1386-1414
    • Korolainen, M.A.1    Nyman, T.A.2    Aittokallio, T.3    Pirttila, T.4
  • 17
    • 0035397916 scopus 로고    scopus 로고
    • Proteomics - Post-genomic cartography to understand gene function
    • Naaby-Hansen, S.; Waterfield, M. D.; Cramer, R. Proteomics-post-genomic cartography to understand gene function Trends Pharmacol. Sci. 2001, 22 (7) 376-384
    • (2001) Trends Pharmacol. Sci. , vol.22 , Issue.7 , pp. 376-384
    • Naaby-Hansen, S.1    Waterfield, M.D.2    Cramer, R.3
  • 19
    • 33749256309 scopus 로고    scopus 로고
    • Methods for proteomics in neuroscience
    • Tannu, N. S.; Hemby, S. E. Methods for proteomics in neuroscience Prog. Brain Res. 2006, 158, 41-82
    • (2006) Prog. Brain Res. , vol.158 , pp. 41-82
    • Tannu, N.S.1    Hemby, S.E.2
  • 20
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann, M.; Hendrickson, R. C.; Pandey, A. Analysis of proteins and proteomes by mass spectrometry Annu. Rev. Biochem. 2001, 70, 437-473
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 21
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J.; Raijmakers, R.; Lemeer, S.; Mohammed, S.; Heck, A. J. R. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics Nat. Protoc. 2009, 4 (4) 484-494
    • (2009) Nat. Protoc. , vol.4 , Issue.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.R.5
  • 23
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1 (5) 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 24
    • 84877131508 scopus 로고    scopus 로고
    • Dimethyl-labeling-based protein quantification and pathway search: A novel method of spinal cord analysis applicable for neurological studies
    • Sui, P.; Watanabe, H.; Ossipov, M. H.; Porreca, F.; Bakalkin, G.; Bergquist, J.; Artemenko, K. Dimethyl-labeling-based protein quantification and pathway search: A novel method of spinal cord analysis applicable for neurological studies J. Proteome Res. 2013, 12 (5) 2245-2252
    • (2013) J. Proteome Res. , vol.12 , Issue.5 , pp. 2245-2252
    • Sui, P.1    Watanabe, H.2    Ossipov, M.H.3    Porreca, F.4    Bakalkin, G.5    Bergquist, J.6    Artemenko, K.7
  • 26
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimers-Disease (Cerad) 0.2. Standardization of the neuropathologic assessment of Alzheimers-disease
    • Mirra, S. S.; Heyman, A.; McKeel, D.; Sumi, S. M.; Crain, B. J.; Brownlee, L. M.; Vogel, F. S.; Hughes, J. P.; Vanbelle, G.; Berg, L. The Consortium to Establish a Registry for Alzheimers-Disease (Cerad) 0.2. Standardization of the neuropathologic assessment of Alzheimers-disease Neurology 1991, 41 (4) 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    Vanbelle, G.9    Berg, L.10
  • 27
    • 79958144961 scopus 로고    scopus 로고
    • Analysis of membrane and hydrophilic proteins simultaneously derived from the mouse brain using cloud-point extraction
    • Wetterhall, M.; Shevchenko, G.; Artemenko, K.; Sjodin, M. O. D.; Bergquist, J. Analysis of membrane and hydrophilic proteins simultaneously derived from the mouse brain using cloud-point extraction Anal. Bioanal. Chem. 2011, 400 (9) 2827-2836
    • (2011) Anal. Bioanal. Chem. , vol.400 , Issue.9 , pp. 2827-2836
    • Wetterhall, M.1    Shevchenko, G.2    Artemenko, K.3    Sjodin, M.O.D.4    Bergquist, J.5
  • 28
    • 0033543717 scopus 로고    scopus 로고
    • Protein delipidation and precipitation by tri-n-butyl phosphate, acetone, and methanol treatment for isoelectric focusing and two-dimensional gel electrophoresis
    • Mastro, R.; Hall, M. Protein delipidation and precipitation by tri-n-butyl phosphate, acetone, and methanol treatment for isoelectric focusing and two-dimensional gel electrophoresis Anal. Biochem. 1999, 273 (2) 313-315
    • (1999) Anal. Biochem. , vol.273 , Issue.2 , pp. 313-315
    • Mastro, R.1    Hall, M.2
  • 30
    • 58849132290 scopus 로고    scopus 로고
    • Medial temporal lobe atrophy on MRI differentiates Alzheimers disease from dementia with Lewy bodies and vascular cognitive impairment: A prospective study with pathological verification of diagnosis
    • Burton, E. J.; Barber, R.; Mukaetova-Ladinska, E. B.; Robson, J.; Perry, R. H.; Jaros, E.; Kalaria, R. N.; Obrien, J. T. Medial temporal lobe atrophy on MRI differentiates Alzheimers disease from dementia with Lewy bodies and vascular cognitive impairment: a prospective study with pathological verification of diagnosis Brain 2009, 132, 195-203
    • (2009) Brain , vol.132 , pp. 195-203
    • Burton, E.J.1    Barber, R.2    Mukaetova-Ladinska, E.B.3    Robson, J.4    Perry, R.H.5    Jaros, E.6    Kalaria, R.N.7    Obrien, J.T.8
  • 32
    • 75149161571 scopus 로고    scopus 로고
    • Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease
    • Sultana, R.; Perluigi, M.; Newman, S. F.; Pierce, W. M.; Cini, C.; Coccia, R.; Butterfield, D. A. Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease Antioxid. Redox Signaling 2010, 12 (3) 327-336
    • (2010) Antioxid. Redox Signaling , vol.12 , Issue.3 , pp. 327-336
    • Sultana, R.1    Perluigi, M.2    Newman, S.F.3    Pierce, W.M.4    Cini, C.5    Coccia, R.6    Butterfield, D.A.7
  • 33
    • 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. M.; Cooper, G. J. S. Proteomic analysis of the brain in Alzheimer's disease: Molecular phenotype of a complex disease process Proteomics 2001, 1 (12) 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.M.4    Cooper, G.J.S.5
  • 34
    • 1542509945 scopus 로고    scopus 로고
    • Cytoskeleton derangement in brain of patients with Down Syndrome, Alzheimer's disease and Pick's disease
    • Pollak, D.; Cairns, N.; Lubec, G. Cytoskeleton derangement in brain of patients with Down Syndrome, Alzheimer's disease and Pick's disease J. Neural Transm., Suppl. 2003, 67, 149-158
    • (2003) J. Neural Transm., Suppl. , vol.67 , pp. 149-158
    • Pollak, D.1    Cairns, N.2    Lubec, G.3
  • 35
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith, M. A.; Harris, P. L.; Sayre, L. M.; Perry, G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals Proc. Natl. Acad. Sci. U.S.A. 1997, 94 (18) 9866-8
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.18 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 38
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M. T.; Beal, M. F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 2006, 443 (7113) 787-795
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 40
    • 50249099760 scopus 로고    scopus 로고
    • ITRAQ analysis of complex proteome alterations in 3xTgAD Alzheimer's mice: Understanding the interface between physiology and disease
    • (e2750
    • Martin, B.; Brenneman, R.; Becker, K. G.; Gucek, M.; Cole, R. N.; Maudsley, S. iTRAQ analysis of complex proteome alterations in 3xTgAD Alzheimer's mice: Understanding the interface between physiology and disease PLoS One 2008, 3 (7 e2750
    • (2008) PLoS One , vol.3 , Issue.7
    • Martin, B.1    Brenneman, R.2    Becker, K.G.3    Gucek, M.4    Cole, R.N.5    Maudsley, S.6
  • 42
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • Bubber, P.; Haroutunian, V.; Fisch, G.; Blass, J. P.; Gibson, G. E. Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications Ann. Neurol. 2005, 57 (5) 695-703
    • (2005) Ann. Neurol. , vol.57 , Issue.5 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Blass, J.P.4    Gibson, G.E.5
  • 43
    • 0029884010 scopus 로고    scopus 로고
    • Brain protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • Mastrogiacomo, F.; Lindsay, J. G.; Bettendorff, L.; Rice, J.; Kish, S. J. Brain protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease Ann. Neurol. 1996, 39 (5) 592-598
    • (1996) Ann. Neurol. , vol.39 , Issue.5 , pp. 592-598
    • Mastrogiacomo, F.1    Lindsay, J.G.2    Bettendorff, L.3    Rice, J.4    Kish, S.J.5
  • 44
    • 0033679409 scopus 로고    scopus 로고
    • Decreased levels of complex III core protein 1 and complex v beta chain in brains from patients with Alzheimer's disease and Down syndrome
    • Kim, S. H.; Vlkolinsky, R.; Cairns, N.; Lubec, G. Decreased levels of complex III core protein 1 and complex V beta chain in brains from patients with Alzheimer's disease and Down syndrome Cell. Mol. Life Sci. 2000, 57 (12) 1810-1816
    • (2000) Cell. Mol. Life Sci. , vol.57 , Issue.12 , pp. 1810-1816
    • Kim, S.H.1    Vlkolinsky, R.2    Cairns, N.3    Lubec, G.4
  • 45
    • 0030681378 scopus 로고    scopus 로고
    • Amyloid angiopathy and blood-brain barrier changes in Alzheimer's disease
    • Wisniewski, H. M.; Vorbrodt, A. W.; Wegiel, J. Amyloid angiopathy and blood-brain barrier changes in Alzheimer's disease Ann. N.Y. Acad. Sci. 1997, 826, 161-172
    • (1997) Ann. N.Y. Acad. Sci. , vol.826 , pp. 161-172
    • Wisniewski, H.M.1    Vorbrodt, A.W.2    Wegiel, J.3
  • 46
    • 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.; 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. 2008, 30 (1) 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
  • 48
    • 0029869755 scopus 로고    scopus 로고
    • Glucose regulation and cognitive functions: Relation to Alzheimer's disease and diabetes
    • Messier, C.; Gagnon, M. Glucose regulation and cognitive functions: relation to Alzheimer's disease and diabetes Behav. Brain Res. 1996, 75 (1-2) 1-11
    • (1996) Behav. Brain Res. , vol.75 , Issue.12 , pp. 1-11
    • Messier, C.1    Gagnon, M.2
  • 50
    • 0034018813 scopus 로고    scopus 로고
    • Apoptosis in Alzheimer's disease - An update
    • Shimohama, S. Apoptosis in Alzheimer's disease - an update Apoptosis 2000, 5 (1) 9-16
    • (2000) Apoptosis , vol.5 , Issue.1 , pp. 9-16
    • Shimohama, S.1
  • 51
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R. D.; Masliah, E.; Salmon, D. P.; Butters, N.; DeTeresa, R.; Hill, R.; Hansen, L. A.; Katzman, R. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment Ann. Neurol. 1991, 30 (4) 572-80
    • (1991) Ann. Neurol. , vol.30 , Issue.4 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 53
    • 84870935048 scopus 로고    scopus 로고
    • Longitudinal characterization of the brain proteomes for the Tg2576 amyloid mouse model using shotgun based mass spectrometry
    • Shevchenko, G.; Wetterhall, M.; Bergquist, J.; Hoglund, K.; Andersson, L. I.; Kultima, K. Longitudinal characterization of the brain proteomes for the Tg2576 amyloid mouse model using shotgun based mass spectrometry J. Proteome Res. 2012, 11 (12) 6159-6174
    • (2012) J. Proteome Res. , vol.11 , Issue.12 , pp. 6159-6174
    • Shevchenko, G.1    Wetterhall, M.2    Bergquist, J.3    Hoglund, K.4    Andersson, L.I.5    Kultima, K.6
  • 55
    • 0030705234 scopus 로고    scopus 로고
    • P28 Bap31, a Bcl-2/Bcl-X-L- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng, F. W. H.; Nguyen, M.; Kwan, T.; Branton, P. E.; Nicholson, D. W.; Cromlish, J. A.; Shore, G. C. p28 Bap31, a Bcl-2/Bcl-X-L- and procaspase-8-associated protein in the endoplasmic reticulum J. Cell Biol. 1997, 139 (2) 327-338
    • (1997) J. Cell Biol. , vol.139 , Issue.2 , pp. 327-338
    • Ng, F.W.H.1    Nguyen, M.2    Kwan, T.3    Branton, P.E.4    Nicholson, D.W.5    Cromlish, J.A.6    Shore, G.C.7
  • 56
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Christen, Y. Oxidative stress and Alzheimer disease Am. J. Clin. Nutr. 2000, 71 (2) 621S-629S
    • (2000) Am. J. Clin. Nutr. , vol.71 , Issue.2
    • Christen, Y.1
  • 57
    • 0141767139 scopus 로고    scopus 로고
    • Proteomics in Alzheimer's disease: Insights into potential mechanisms of neurodegeneration
    • Butterfield, D. A.; Boyd-Kimball, D.; Castegna, A. Proteomics in Alzheimer's disease: insights into potential mechanisms of neurodegeneration J. Neurochem. 2003, 86 (6) 1313-27
    • (2003) J. Neurochem. , vol.86 , Issue.6 , pp. 1313-1327
    • Butterfield, D.A.1    Boyd-Kimball, D.2    Castegna, A.3
  • 58
    • 0037015001 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage
    • Manevich, Y.; Sweitzer, T.; Pak, J. H.; Feinstein, S. I.; Muzykantov, V.; Fisher, A. B. 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage Proc. Natl. Acad. Sci. U.S.A. 2002, 99 (18) 11599-604
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.18 , pp. 11599-11604
    • Manevich, Y.1    Sweitzer, T.2    Pak, J.H.3    Feinstein, S.I.4    Muzykantov, V.5    Fisher, A.B.6
  • 59
    • 0042090273 scopus 로고    scopus 로고
    • Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress
    • Wang, X.; Phelan, S. A.; Forsman-Semb, K.; Taylor, E. F.; Petros, C.; Brown, A.; Lerner, C. P.; Paigen, B. Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress J. Biol. Chem. 2003, 278 (27) 25179-90
    • (2003) J. Biol. Chem. , vol.278 , Issue.27 , pp. 25179-25190
    • Wang, X.1    Phelan, S.A.2    Forsman-Semb, K.3    Taylor, E.F.4    Petros, C.5    Brown, A.6    Lerner, C.P.7    Paigen, B.8
  • 60
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • Yoo, B. C.; Kim, S. H.; Cairns, N.; Fountoulakis, M.; Lubec, G. Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease Biochem. Biophys. Res. Commun. 2001, 280 (1) 249-58
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , Issue.1 , pp. 249-258
    • Yoo, B.C.1    Kim, S.H.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 62
    • 0035140070 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase activity is required for the expression of glial fibrillary acidic protein upon cAMP-dependent induction of differentiation in rat C6 glioma
    • Roymans, D.; Vissenberg, K.; De Jonghe, C.; Grobben, B.; Claes, P.; Verbelen, J. P.; Van Broeckhoven, C.; Slegers, H. Phosphatidylinositol 3-kinase activity is required for the expression of glial fibrillary acidic protein upon cAMP-dependent induction of differentiation in rat C6 glioma J. Neurochem. 2001, 76 (2) 610-618
    • (2001) J. Neurochem. , vol.76 , Issue.2 , pp. 610-618
    • Roymans, D.1    Vissenberg, K.2    De Jonghe, C.3    Grobben, B.4    Claes, P.5    Verbelen, J.P.6    Van Broeckhoven, C.7    Slegers, H.8
  • 63
    • 1842528400 scopus 로고    scopus 로고
    • Convergence of atherosclerosis and Alzheimer's disease: Inflammation, cholesterol, and misfolded proteins
    • Casserly, I.; Topol, E. Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins Lancet 2004, 363 (9415) 1139-46
    • (2004) Lancet , vol.363 , Issue.9415 , pp. 1139-1146
    • Casserly, I.1    Topol, E.2
  • 64
    • 0028102760 scopus 로고
    • The lipocalin protein family - A role in cell regulation
    • Flower, D. R. The lipocalin protein family-A role in cell regulation FEBS Lett. 1994, 354 (1) 7-11
    • (1994) FEBS Lett. , vol.354 , Issue.1 , pp. 7-11
    • Flower, D.R.1
  • 65
    • 28244433804 scopus 로고    scopus 로고
    • Apolipoproteins and their role in different clinical conditions: An overview
    • Irshad, M.; Dubey, R. Apolipoproteins and their role in different clinical conditions: an overview Indian J. Biochem. Biophys. 2005, 42 (2) 73-80
    • (2005) Indian J. Biochem. Biophys. , vol.42 , Issue.2 , pp. 73-80
    • Irshad, M.1    Dubey, R.2
  • 66
    • 0031658643 scopus 로고    scopus 로고
    • Increased levels of apolipoprotein D in cerebrospinal fluid and hippocampus of Alzheimer's patients
    • Terrisse, L.; Poirier, J.; Bertrand, P.; Merched, A.; Visvikis, S.; Siest, G.; Milne, R.; Rassart, E. Increased levels of apolipoprotein D in cerebrospinal fluid and hippocampus of Alzheimer's patients J. Neurochem. 1998, 71 (4) 1643-1650
    • (1998) J. Neurochem. , vol.71 , Issue.4 , pp. 1643-1650
    • Terrisse, L.1    Poirier, J.2    Bertrand, P.3    Merched, A.4    Visvikis, S.5    Siest, G.6    Milne, R.7    Rassart, E.8
  • 67
  • 68
  • 70
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T. C. The synaptic vesicle cycle Annu. Rev. Neurosci. 2004, 27, 509-547
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 71
    • 0033230745 scopus 로고    scopus 로고
    • Essential roles in synaptic plasticity for synaptogyrin i and synaptophysin i
    • Janz, R.; Sudhof, T. C.; Hammer, R. E.; Unni, V.; Siegelbaum, S. A.; Bolshakov, V. Y. Essential roles in synaptic plasticity for synaptogyrin I and synaptophysin I Neuron 1999, 24 (3) 687-700
    • (1999) Neuron , vol.24 , Issue.3 , pp. 687-700
    • Janz, R.1    Sudhof, T.C.2    Hammer, R.E.3    Unni, V.4    Siegelbaum, S.A.5    Bolshakov, V.Y.6
  • 72
    • 79959985842 scopus 로고    scopus 로고
    • Age-Related Changes in Gene Expression are Accelerated in Alzheimer's Disease
    • Saetre, P.; Jazin, E.; Emilsson, L. Age-Related Changes in Gene Expression are Accelerated in Alzheimer's Disease Synapse 2011, 65 (9) 971-974
    • (2011) Synapse , vol.65 , Issue.9 , pp. 971-974
    • Saetre, P.1    Jazin, E.2    Emilsson, L.3
  • 73
    • 60249089296 scopus 로고    scopus 로고
    • Biochemical characterization of tau protein and its associated syndapin 1 and protein kinase Cepsilon for their functional regulation in rat brain
    • Suzuki, K.; Kawakami, F.; Sasaki, H.; Maruyama, H.; Ohtsuki, K. Biochemical characterization of tau protein and its associated syndapin 1 and protein kinase Cepsilon for their functional regulation in rat brain Biochim. Biophys. Acta 2009, 1790 (3) 188-97
    • (2009) Biochim. Biophys. Acta , vol.1790 , Issue.3 , pp. 188-197
    • Suzuki, K.1    Kawakami, F.2    Sasaki, H.3    Maruyama, H.4    Ohtsuki, K.5
  • 74
    • 0028063607 scopus 로고
    • Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies
    • Martin, H.; Rostas, J.; Patel, Y.; Aitken, A. Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies J. Neurochem. 1994, 63 (6) 2259-65
    • (1994) J. Neurochem. , vol.63 , Issue.6 , pp. 2259-2265
    • Martin, H.1    Rostas, J.2    Patel, Y.3    Aitken, A.4
  • 75
    • 84862501132 scopus 로고    scopus 로고
    • 14-3-3 proteins in neurological disorders
    • Foote, M.; Zhou, Y. 14-3-3 proteins in neurological disorders Int J Biochem Mol Biol 2012, 3 (2) 152-64
    • (2012) Int J Biochem Mol Biol , vol.3 , Issue.2 , pp. 152-164
    • Foote, M.1    Zhou, Y.2
  • 77
    • 0026727853 scopus 로고
    • Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling
    • Maycox, P. R.; Link, E.; Reetz, A.; Morris, S. A.; Jahn, R. Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling J. Cell Biol. 1992, 118 (6) 1379-88
    • (1992) J. Cell Biol. , vol.118 , Issue.6 , pp. 1379-1388
    • Maycox, P.R.1    Link, E.2    Reetz, A.3    Morris, S.A.4    Jahn, R.5
  • 79
    • 79957457516 scopus 로고    scopus 로고
    • Impairment of the activity of the plasma membrane Ca2+-ATPase in Alzheimer's disease
    • Mata, A. M.; Berrocal, M.; Sepulveda, M. R. Impairment of the activity of the plasma membrane Ca2+-ATPase in Alzheimer's disease Biochem. Soc. Trans. 2011, 39, 819-822
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 819-822
    • Mata, A.M.1    Berrocal, M.2    Sepulveda, M.R.3
  • 80
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny, I.; Mattson, M. P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease Trends Neurosci. 2008, 31 (9) 454-463
    • (2008) Trends Neurosci. , vol.31 , Issue.9 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 83
    • 0034681926 scopus 로고    scopus 로고
    • Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522
    • Gu, Y.; Hamajima, N.; Ihara, Y. Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522 Biochemistry 2000, 39 (15) 4267-75
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4267-4275
    • Gu, Y.1    Hamajima, N.2    Ihara, Y.3
  • 84
    • 84866857074 scopus 로고    scopus 로고
    • Do proteomics analyses provide insights into reduced oxidative stress in the brain of an Alzheimer disease transgenic mouse model with an M631L amyloid precursor protein substitution and thereby the importance of amyloid-beta-resident methionine 35 in Alzheimer disease pathogenesis?
    • Sultana, R.; Robinson, R. A.; Lange, M. B.; Fiorini, A.; Galvan, V.; Fombonne, J.; Baker, A.; Gorostiza, O.; Zhang, J.; Cai, J.; Pierce, W. M.; Bredesen, D. E.; Butterfield, D. A. Do proteomics analyses provide insights into reduced oxidative stress in the brain of an Alzheimer disease transgenic mouse model with an M631L amyloid precursor protein substitution and thereby the importance of amyloid-beta-resident methionine 35 in Alzheimer disease pathogenesis? Antioxid. Redox. Signal. 2012, 17 (11) 1507-14
    • (2012) Antioxid. Redox. Signal. , vol.17 , Issue.11 , pp. 1507-1514
    • Sultana, R.1    Robinson, R.A.2    Lange, M.B.3    Fiorini, A.4    Galvan, V.5    Fombonne, J.6    Baker, A.7    Gorostiza, O.8    Zhang, J.9    Cai, J.10    Pierce, W.M.11    Bredesen, D.E.12    Butterfield, D.A.13
  • 85
    • 0034071656 scopus 로고    scopus 로고
    • Growth-associated protein GAP-43 in the frontal cortex and in the hippocampus in Alzheimer's disease: An immunohistochemical and quantitative study
    • Bogdanovic, N.; Davidsson, P.; Volkmann, I.; Winblad, B.; Blennow, K. Growth-associated protein GAP-43 in the frontal cortex and in the hippocampus in Alzheimer's disease: an immunohistochemical and quantitative study J. Neural Transm. 2000, 107 (4) 463-78
    • (2000) J. Neural Transm. , vol.107 , Issue.4 , pp. 463-478
    • Bogdanovic, N.1    Davidsson, P.2    Volkmann, I.3    Winblad, B.4    Blennow, K.5
  • 86
    • 33750982682 scopus 로고    scopus 로고
    • Cathepsin D-mediated proteolysis of apolipoprotein E: Possible role in Alzheimer's disease
    • Zhou, W.; Scott, S. A.; Shelton, S. B.; Crutcher, K. A. Cathepsin D-mediated proteolysis of apolipoprotein E: possible role in Alzheimer's disease Neuroscience 2006, 143 (3) 689-701
    • (2006) Neuroscience , vol.143 , Issue.3 , pp. 689-701
    • Zhou, W.1    Scott, S.A.2    Shelton, S.B.3    Crutcher, K.A.4
  • 87
    • 67049137065 scopus 로고    scopus 로고
    • Cell adhesion molecules in the central nervous system
    • Togashi, H.; Sakisaka, T.; Takai, Y. Cell adhesion molecules in the central nervous system Cell. Adhes. Migr. 2009, 3 (1) 29-35
    • (2009) Cell. Adhes. Migr. , vol.3 , Issue.1 , pp. 29-35
    • Togashi, H.1    Sakisaka, T.2    Takai, Y.3
  • 89
    • 0042387935 scopus 로고    scopus 로고
    • Human Abeta1-42 reduces iron-induced toxicity in rat cerebral cortex
    • Bishop, G. M.; Robinson, S. R. Human Abeta1-42 reduces iron-induced toxicity in rat cerebral cortex J. Neurosci. Res. 2003, 73 (3) 316-23
    • (2003) J. Neurosci. Res. , vol.73 , Issue.3 , pp. 316-323
    • Bishop, G.M.1    Robinson, S.R.2
  • 90
    • 84880137264 scopus 로고    scopus 로고
    • Ferritin light chain interacts with PEN-2 and affects gamma-secretase activity
    • Li, X.; Liu, Y.; Zheng, Q.; Yao, G.; Cheng, P.; Bu, G.; Xu, H.; Zhang, Y. W. Ferritin light chain interacts with PEN-2 and affects gamma-secretase activity Neurosci. Lett. 2013, 548, 90-4
    • (2013) Neurosci. Lett. , vol.548 , pp. 90-94
    • Li, X.1    Liu, Y.2    Zheng, Q.3    Yao, G.4    Cheng, P.5    Bu, G.6    Xu, H.7    Zhang, Y.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.