메뉴 건너뛰기




Volumn 39, Issue 1, 2014, Pages 208-215

Differential expression of proteins in brain regions of alzheimer's disease patients

Author keywords

Alzheimer's disease; Cortex; Hippocampus; Neurodegeneration; Proteomics; Substantia nigra

Indexed keywords

ACONITATE HYDRATASE; CALBINDIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN; CREATINE KINASE; DIHYDROLIPOAMIDE DEHYDROGENASE; ELONGATION FACTOR TU; FASCIN; FUMARATE HYDRATASE; GLIAL FIBRILLARY ACIDIC PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANINE DEAMINASE; HEAT SHOCK PROTEIN; ISOCITRATE DEHYDROGENASE; LACTATE DEHYDROGENASE ISOENZYME 1; LACTOYLGLUTATHIONE LYASE; LANC LIKE PROTEIN 1; LIPOCORTIN 5; MALATE DEHYDROGENASE; N ETHYLMALEIMIDE SENSITIVE FACTOR; NUCLEOSIDE DIPHOSPHATE KINASE; NUCLEOSIDE DIPHOSPHATE KINASE B; PROLYL ENDOPEPTIDASE; PROTEIN 14 3 3; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SYNAPSIN; SYNAPSIN I; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; UNCLASSIFIED DRUG; UNINDEXED DRUG; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 84892677529     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-013-1210-1     Document Type: Article
Times cited : (34)

References (29)
  • 2
    • 77953826456 scopus 로고    scopus 로고
    • Analysis of the cellular Aspergillus fumigatus proteome that reacts with sera from rabbits developing an acquired immunity after experimental aspergillosis
    • 1:CAS:528:DC%2BC3cXnvFSis7g%3D 20564691 10.1002/elps.201000015
    • Asif AR, Oellerich M, Amstrong VW, Gross U, Reichard U (2010) Analysis of the cellular Aspergillus fumigatus proteome that reacts with sera from rabbits developing an acquired immunity after experimental aspergillosis. Electrophoresis 31:1947-1958
    • (2010) Electrophoresis , vol.31 , pp. 1947-1958
    • Asif, A.R.1    Oellerich, M.2    Amstrong, V.W.3    Gross, U.4    Reichard, U.5
  • 4
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • 1:CAS:528:DyaL2sXhsFagtLc%3D 10.1002/elps.1150080203
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 5
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • 1:STN:280:DyaK387gtFOiug%3D%3D 1759558 10.1007/BF00308809
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82:239-259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 6
    • 33646340668 scopus 로고    scopus 로고
    • The creatine kinase/creatine connection to Alzheimer's disease: CK-inactivation, APP-CK complexes and focal creatine deposits
    • Bürklen TS, Schlattner U, Homayouni R, Gough K, Rak M, Szeghalmi A, Wallimann T (2006) The creatine kinase/creatine connection to Alzheimer's disease: CK-inactivation, APP-CK complexes and focal creatine deposits. J Biomed Biotechnol 2006:35936
    • (2006) J Biomed Biotechnol , vol.2006 , pp. 35936
    • Bürklen Ts, S.1
  • 8
    • 13844318224 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases
    • DOI 10.1146/annurev.pharmtox.45.120403.095902
    • Chuang DM, Hough C, Senatorov VV (2005) Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases. Annu Rev Pharmacol Toxicol 45:269-290 (Pubitemid 40261806)
    • (2005) Annual Review of Pharmacology and Toxicology , vol.45 , pp. 269-290
    • Chuang, D.-M.1    Hough, C.2    Senatorov, V.V.3
  • 9
    • 28744448949 scopus 로고    scopus 로고
    • Amyloid-β induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease
    • DOI 10.1096/fj.05-4195fje
    • Cumming RC, Schubert D (2005) Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease. FASEB J 19:2060-2062 (Pubitemid 41759765)
    • (2005) FASEB Journal , vol.19 , Issue.14 , pp. 2060-2062
    • Cumming, R.C.1    Schubert, D.2
  • 10
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease
    • DOI 10.1016/0022-510X(87)90057-8
    • Davies CA, Mann DM, Sumpter PQ, Yates PO (1987) A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. J Neurol Sci 78:151-164 (Pubitemid 17031709)
    • (1987) Journal of the Neurological Sciences , vol.78 , Issue.2 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.A.2    Sumpter, P.Q.3    Yates, P.O.4
  • 11
    • 77957994659 scopus 로고    scopus 로고
    • Multiple defects in energy metabolism in Alzheimer's disease
    • 1:CAS:528:DC%2BC3MXptVCgu7w%3D 20840064 10.2174/1389450111007011193
    • Ferreira IL, Resende R, Ferreiro E, Ergo AC, Pereira CF (2010) Multiple defects in energy metabolism in Alzheimer's disease. Curr Drug Targets 11:1193-1206
    • (2010) Curr Drug Targets , vol.11 , pp. 1193-1206
    • Ferreira, I.L.1    Resende, R.2    Ferreiro, E.3    Ergo, A.C.4    Pereira, C.F.5
  • 12
    • 18244389436 scopus 로고    scopus 로고
    • The role of cerebral amyloid β accumulation in common forms of Alzheimer disease
    • DOI 10.1172/JCI200525100
    • Gandy S (2005) The role of cerebral amyloid beta accumulation in common forms of Alzheimer disease. J Clin Invest 115:1121-1129 (Pubitemid 40629026)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.5 , pp. 1121-1129
    • Gandy, S.1
  • 13
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • DOI 10.1016/S0960-9822(02)01184-3, PII S0960982202011843
    • Gohla A, Bokoch GM (2002) 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12:1704-1710 (Pubitemid 35161927)
    • (2002) Current Biology , vol.12 , Issue.19 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 14
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S, Hipolito A, Saffer L (1998) Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J Neurosci 18:9835-9844 (Pubitemid 28543762)
    • (1998) Journal of Neuroscience , vol.18 , Issue.23 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 15
    • 79953854897 scopus 로고    scopus 로고
    • Alzheimer's disease: The challenge of the second century
    • Holtzman DM, Morris JC, Goate AM (2011) Alzheimer's disease: the challenge of the second century. Sci Transl Med 3:77sr1
    • (2011) Sci Transl Med , vol.3
    • Holtzman, D.M.1    Morris, J.C.2    Goate, A.M.3
  • 17
    • 0035145627 scopus 로고    scopus 로고
    • Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts
    • DOI 10.1046/j.1471-4159.2001.00033.x
    • Mazzola JL, Sirover MA (2001) Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. J Neurochem 76:442-449 (Pubitemid 32097022)
    • (2001) Journal of Neurochemistry , vol.76 , Issue.2 , pp. 442-449
    • Mazzola, J.L.1    Sirover, M.A.2
  • 18
    • 54549093577 scopus 로고    scopus 로고
    • Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures
    • 1:CAS:528:DC%2BD1cXhtlaqtbzN 18725330 10.1016/j.bbapap.2008.07.013
    • Naletova I, Schmalhausen E, Kharitonov A, Katrukha A, Saso L, Caprioli A, Muronetz V (2008) Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures. Biochim Biophys Acta 1784:2052-2058
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 2052-2058
    • Naletova, I.1    Schmalhausen, E.2    Kharitonov, A.3    Katrukha, A.4    Saso, L.5    Caprioli, A.6    Muronetz, V.7
  • 19
    • 85027949706 scopus 로고    scopus 로고
    • Tau mediated neurodegeneration: An insight into Alzheimer's disease pathology
    • 1:CAS:528:DC%2BC3MXkvFeisbg%3D 21509508 10.1007/s11064-011-0475-5
    • Obulesu M, Venu R, Somashekhar R (2011) Tau mediated neurodegeneration: an insight into Alzheimer's disease pathology. Neurochem Res 36:1329-1335
    • (2011) Neurochem Res , vol.36 , pp. 1329-1335
    • Obulesu, M.1    Venu, R.2    Somashekhar, R.3
  • 20
    • 12144289492 scopus 로고    scopus 로고
    • Alterations in Glucose Metabolism Induce Hypothermia Leading to Tau Hyperphosphorylation through Differential Inhibition of Kinase and Phosphatase Activities: Implications for Alzheimer's Disease
    • DOI 10.1523/JNEUROSCI.5561-03.2004
    • Planel E, Miyasaka T, Launey T, Chui DH, Tanemura K, Sato S, Murayama O, Ishiguro K, Tatebayashi Y, Takashima A (2004) Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: implications for Alzheimer's disease. J Neurosci 24:2401-2411 (Pubitemid 38327953)
    • (2004) Journal of Neuroscience , vol.24 , Issue.10 , pp. 2401-2411
    • Planel, E.1    Miyasaka, T.2    Launey, T.3    Chui, D.-H.4    Tanemura, K.5    Sato, S.6    Murayama, O.7    Ishiguro, K.8    Tatebayashi, Y.9    Takashima, A.10
  • 22
    • 79952574501 scopus 로고    scopus 로고
    • Epidemiology of Alzheimer disease
    • 3339565 21304480 10.1038/nrneurol.2011.2
    • Reitz C, Brayne C, Mayeux R (2011) Epidemiology of Alzheimer disease. Nat Rev Neurol 7:137-152
    • (2011) Nat Rev Neurol , vol.7 , pp. 137-152
    • Reitz, C.1    Brayne, C.2    Mayeux, R.3
  • 23
    • 68149148549 scopus 로고    scopus 로고
    • Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells
    • 1:CAS:528:DC%2BD1MXptFClurw%3D 19350381 10.1007/s10571-009-9398-y
    • Rhein V, Baysang G, Rao S, Meier F, Bonert A, Müller-Spahn F, Eckert A (2009) Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells. Cell Mol Neurobiol 29:1063-1071
    • (2009) Cell Mol Neurobiol , vol.29 , pp. 1063-1071
    • Rhein, V.1    Baysang, G.2    Rao, S.3    Meier, F.4    Bonert, A.5    Müller-Spahn, F.6    Eckert, A.7
  • 24
    • 0024809382 scopus 로고
    • Neuronal loss in the substantia nigra in patients with Alzheimer's disease and Parkinson's disease in relation to extrapyramidal symptoms and dementia
    • 1:STN:280:DyaK3c%2FpvFCkug%3D%3D 2602422
    • Rinne JO, Rummukainen J, Paljärvi L, Säkö E, Mölsä P, Rinne UK (1989) Neuronal loss in the substantia nigra in patients with Alzheimer's disease and Parkinson's disease in relation to extrapyramidal symptoms and dementia. Prog Clin Biol Res 317:325-332
    • (1989) Prog Clin Biol Res , vol.317 , pp. 325-332
    • Rinne, J.O.1    Rummukainen, J.2    Paljärvi, L.3    Säkö, E.4    Mölsä, P.5    Rinne, U.K.6
  • 25
    • 0032752399 scopus 로고    scopus 로고
    • Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0014-5793(99)01383-6, PII S0014579399013836
    • Roth D, Birkenfeld J (1999) Betz H dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett 460:411-416 (Pubitemid 29518410)
    • (1999) FEBS Letters , vol.460 , Issue.3 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 27
    • 4844230325 scopus 로고    scopus 로고
    • 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease
    • DOI 10.1007/s00401-004-0885-4
    • Umahara T, Uchihara T, Tsuchiya K, Nakamura A, Iwamoto T, Ikeda K, Takasaki M (2004) 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol 108:279-286 (Pubitemid 39317695)
    • (2004) Acta Neuropathologica , vol.108 , Issue.4 , pp. 279-286
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3    Nakamura, A.4    Iwamoto, T.5    Ikeda, K.6    Takasaki, M.7
  • 28
    • 40749153440 scopus 로고    scopus 로고
    • Proteome analysis of human substantia nigra in Parkinson's disease
    • DOI 10.1186/1477-5956-6-8
    • Werner CJ, Heyny-von Haussen R, Mall G, Wolf S (2008) Proteome analysis of human substantia nigra in Parkinson's disease. Proteome Sci 6:8 (Pubitemid 351385673)
    • (2008) Proteome Science , vol.6 , pp. 8
    • Werner, C.J.1    Heyny-von Haussen, R.2    Mall, G.3    Wolf, S.4
  • 29
    • 84862004983 scopus 로고    scopus 로고
    • Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer's disease patients
    • 1:CAS:528:DC%2BC38XhtVGltrnJ 22436009 10.1111/j.1471-4159.2012.07737.x
    • Zahid S, Oellerich M, Asif AR, Ahmed N (2012) Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer's disease patients. J Neurochem 121:954-963
    • (2012) J Neurochem , vol.121 , pp. 954-963
    • Zahid, S.1    Oellerich, M.2    Asif, A.R.3    Ahmed, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.