메뉴 건너뛰기




Volumn 63, Issue 10, 2004, Pages 1080-1091

Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis

Author keywords

Alzheimer disease; Amyloid; Brain; Methylation; Methyltransferase; PP2A; Tau

Indexed keywords

METHYLTRANSFERASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN ABALPHAC; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 5644293035     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnen/63.10.1080     Document Type: Article
Times cited : (183)

References (50)
  • 1
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • Sontag E. Protein phosphatase 2A: The Trojan Horse of cellular signaling. Cell Signal 2001;13:7-16
    • (2001) Cell Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 2
    • 0028885494 scopus 로고
    • Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase
    • Goedert M, Jakes R, Qi Z, Wang JH, Cohen P. Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase. J Neurochem 1995;65:2804-7
    • (1995) J Neurochem , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 3
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A
    • Sontag E, Nunbhakdi-Craig V, Lee G, Bloom GS, Mumby MC. Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron 1996;17:1201-7
    • (1996) Neuron , vol.17 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 4
    • 0029349353 scopus 로고
    • Flicking the switches: Phosphorylation of serine/ threonine protein phosphatases
    • Brautigan DL. Flicking the switches: Phosphorylation of serine/ threonine protein phosphatases. Semin Cancer Biol 1995;6:211-17
    • (1995) Semin Cancer Biol , vol.6 , pp. 211-217
    • Brautigan, D.L.1
  • 5
    • 0030821233 scopus 로고    scopus 로고
    • Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen
    • Ogris E, Gibson DM, Pallas DC. Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen. Oncogene 1997;15:911-17
    • (1997) Oncogene , vol.15 , pp. 911-917
    • Ogris, E.1    Gibson, D.M.2    Pallas, D.C.3
  • 6
    • 0033560729 scopus 로고    scopus 로고
    • Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit
    • Bryant JC, Westphal RS, Wadzinski BE. Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit. Biochem J 1999;339:241-46
    • (1999) Biochem J , vol.339 , pp. 241-246
    • Bryant, J.C.1    Westphal, R.S.2    Wadzinski, B.E.3
  • 7
    • 0033738776 scopus 로고    scopus 로고
    • Mutation of the C-terminal leucine residue of PP2Ac inhibits PR55/B subunit binding and confers supersensitivity to microtubule destabilization in Saccharomyces cerevisiae
    • Evans DR, Hemmings BA. Mutation of the C-terminal leucine residue of PP2Ac inhibits PR55/B subunit binding and confers supersensitivity to microtubule destabilization in Saccharomyces cerevisiae. Mol Gen Genet 2000;264:425-32
    • (2000) Mol Gen Genet , vol.264 , pp. 425-432
    • Evans, D.R.1    Hemmings, B.A.2
  • 8
    • 0034331359 scopus 로고    scopus 로고
    • Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
    • Tolstykh T, Lee J, Vafai S, Stock JB. Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits. EMBO J 2000;19:5682-91
    • (2000) EMBO J , vol.19 , pp. 5682-5691
    • Tolstykh, T.1    Lee, J.2    Vafai, S.3    Stock, J.B.4
  • 9
    • 0034331296 scopus 로고    scopus 로고
    • Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
    • Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J 2000;19:5672-81
    • (2000) EMBO J , vol.19 , pp. 5672-5681
    • Wu, J.1    Tolstykh, T.2    Lee, J.3    Boyd, K.4    Stock, J.B.5    Broach, J.R.6
  • 10
    • 0035177048 scopus 로고    scopus 로고
    • Methylation of the protein phosphatase 2A catalytic subunit is essential for association of balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen
    • Yu XX, Du X, Moreno CS, et al. Methylation of the protein phosphatase 2A catalytic subunit is essential for association of balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen. Mol Biol Cell 2001;12:185-99
    • (2001) Mol Biol Cell , vol.12 , pp. 185-199
    • Yu, X.X.1    Du, X.2    Moreno, C.S.3
  • 11
    • 0035846951 scopus 로고    scopus 로고
    • Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p
    • Wei H, Ashby DG, Moreno CS, et al. Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. J Biol Chem 2001;276:1570-77
    • (2001) J Biol Chem , vol.276 , pp. 1570-1577
    • Wei, H.1    Ashby, D.G.2    Moreno, C.S.3
  • 12
    • 0027184102 scopus 로고
    • Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase
    • Lee J, Stock J. Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase. J Biol Chem 1993;268:19192-95
    • (1993) J Biol Chem , vol.268 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 13
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue
    • De Baere I, Derua R, Janssens V, et al. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry 1999;38:16539-47
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • De Baere, I.1    Derua, R.2    Janssens, V.3
  • 14
    • 0036421097 scopus 로고    scopus 로고
    • Chaperonin assisted overexpression, purification, and characterisation of human PP2A methyltransferase
    • George RR, Harris R, Nunn CM, Cramer R, Djordjevic S. Chaperonin assisted overexpression, purification, and characterisation of human PP2A methyltransferase. Protein Expr Purif 2002;26:266-74
    • (2002) Protein Expr Purif , vol.26 , pp. 266-274
    • George, R.R.1    Harris, R.2    Nunn, C.M.3    Cramer, R.4    Djordjevic, S.5
  • 15
    • 0028154020 scopus 로고
    • Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain
    • Xie H, Clarke S. Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain. J Biol Chem 1994;269:1981-84
    • (1994) J Biol Chem , vol.269 , pp. 1981-1984
    • Xie, H.1    Clarke, S.2
  • 16
    • 0029952559 scopus 로고    scopus 로고
    • A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
    • Lee J, Chen Y, Tolstykh T, Stock J. A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain. Proc Natl Acad Sci U S A 1996;93:6043-47
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6043-6047
    • Lee, J.1    Chen, Y.2    Tolstykh, T.3    Stock, J.4
  • 17
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2a
    • Ogris E, Du X, Nelson KC, et al. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2a. J Biol Chem 1999;274:14382-91
    • (1999) J Biol Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3
  • 18
    • 10744229024 scopus 로고    scopus 로고
    • Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity
    • Leulliot N, Quevillon-Cheruel S, Sorel I, et al. Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity. J Biol Chem 2004;279:8351-58
    • (2004) J Biol Chem , vol.279 , pp. 8351-8358
    • Leulliot, N.1    Quevillon-Cheruel, S.2    Sorel, I.3
  • 19
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin JL, McMillan FM. SAM (dependent) I AM: The S-adenosylmethionine- dependent methyltransferase fold. Curr Opin Struct Biol 2002;12:783-93
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 20
    • 0038575234 scopus 로고    scopus 로고
    • S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin?
    • Frey PA, Magnusson OT. S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem Rev 2003;103:2129-48
    • (2003) Chem Rev , vol.103 , pp. 2129-2148
    • Frey, P.A.1    Magnusson, O.T.2
  • 21
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins S, Crameri A, Evans DR, Hemmings BA, Nitsch RM, Gotz J. Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J Biol Chem 2001;276:38193-200
    • (2001) J Biol Chem , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Gotz, J.6
  • 22
    • 0028786849 scopus 로고
    • Paired helical filament-like phosphorylation of tau, deposition of beta/A4-amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A
    • Arendt T, Holzer M, Fruth R, Bruckner MK, Gartner U. Paired helical filament-like phosphorylation of tau, deposition of beta/A4-amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A. Neuroscience 1995;69:691-98
    • (1995) Neuroscience , vol.69 , pp. 691-698
    • Arendt, T.1    Holzer, M.2    Fruth, R.3    Bruckner, M.K.4    Gartner, U.5
  • 23
    • 0032702875 scopus 로고    scopus 로고
    • Neurotoxic and synaptic effects of okadaic acid, an inhibitor of protein phosphatases
    • Tapia R, Pena F, Arias C. Neurotoxic and synaptic effects of okadaic acid, an inhibitor of protein phosphatases. Neurochem Res 1999;24:1423-30
    • (1999) Neurochem Res , vol.24 , pp. 1423-1430
    • Tapia, R.1    Pena, F.2    Arias, C.3
  • 24
    • 0035666080 scopus 로고    scopus 로고
    • Spatial memory deficit and neurodegeneration induced by the direct injection of okadaic acid into the hippocampus in rats
    • He J, Yamada K, Zou LB, Nabeshima T. Spatial memory deficit and neurodegeneration induced by the direct injection of okadaic acid into the hippocampus in rats. J Neural Transm 2001;108:1435-43
    • (2001) J Neural Transm , vol.108 , pp. 1435-1443
    • He, J.1    Yamada, K.2    Zou, L.B.3    Nabeshima, T.4
  • 25
    • 0035823496 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse
    • Planel E, Yasutake K, Fujita SC, Ishiguro K. Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse. J Biol Chem 2001;276:34298-306
    • (2001) J Biol Chem , vol.276 , pp. 34298-34306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 26
    • 0036769791 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase in Alzheimer's disease
    • Tian Q, Wang J. Role of serine/threonine protein phosphatase in Alzheimer's disease. Neurosignals 2002;11:262-69
    • (2002) Neurosignals , vol.11 , pp. 262-269
    • Tian, Q.1    Wang, J.2
  • 28
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V, Schuck T, Trojanowski JQ, Lee VM. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 2001;168:402-12
    • (2001) Exp Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 29
    • 0346848898 scopus 로고    scopus 로고
    • Impairment of phosphatase 2A contributes to the prolonged MAP kinase phosphorylation in Alzheimer's disease fibroblasts
    • Zhao WQ, Feng C, Alkon DL. Impairment of phosphatase 2A contributes to the prolonged MAP kinase phosphorylation in Alzheimer's disease fibroblasts. Neurobiol Dis 2003;14:458-69
    • (2003) Neurobiol Dis , vol.14 , pp. 458-469
    • Zhao, W.Q.1    Feng, C.2    Alkon, D.L.3
  • 30
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology
    • Sontag E, Luangpirom A, Hladik C, et al. Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology. J Neuropathol Exp Neurol 2004;63:287-301
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 287-301
    • Sontag, E.1    Luangpirom, A.2    Hladik, C.3
  • 31
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • Gong CX, Shaikh S, Wang JZ, Zaidi T, Grundke-Iqbal I, Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain. J Neurochem 1995;65:732-38
    • (1995) J Neurochem , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 32
    • 0033792070 scopus 로고    scopus 로고
    • Structural and functional implications of tau hyperphosphorylation: Information from phosphorylation-mimicking mutated tau proteins
    • Eidenmuller J, Fath T, Hellwig A, Reed J, Sontag E, Brandt R. Structural and functional implications of tau hyperphosphorylation: Information from phosphorylation-mimicking mutated tau proteins. Biochemistry 2000;39:13166-75
    • (2000) Biochemistry , vol.39 , pp. 13166-13175
    • Eidenmuller, J.1    Fath, T.2    Hellwig, A.3    Reed, J.4    Sontag, E.5    Brandt, R.6
  • 33
    • 0029799427 scopus 로고    scopus 로고
    • Brain S-adenosylmethionine levels are severely decreased in Alzheimer's disease
    • Morrison LD, Smith DD, Kish SJ. Brain S-adenosylmethionine levels are severely decreased in Alzheimer's disease. J Neurochem 1996;67:1328-31
    • (1996) J Neurochem , vol.67 , pp. 1328-1331
    • Morrison, L.D.1    Smith, D.D.2    Kish, S.J.3
  • 34
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, et al. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991;41:479-86
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3
  • 35
    • 0027411093 scopus 로고
    • Making the diagnosis of Alzheimer's disease. A primer for practicing pathologists
    • Mirra SS, Hart MN, Terry RD. Making the diagnosis of Alzheimer's disease. A primer for practicing pathologists. Arch Pathol Lab Med 1993;117:132-44
    • (1993) Arch Pathol Lab Med , vol.117 , pp. 132-144
    • Mirra, S.S.1    Hart, M.N.2    Terry, R.D.3
  • 36
    • 0028361380 scopus 로고
    • The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo
    • Favre B, Zolnierowicz S, Turowski P, Hemmings BA. The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. J Biol Chem 1994;269:16311-17
    • (1994) J Biol Chem , vol.269 , pp. 16311-16317
    • Favre, B.1    Zolnierowicz, S.2    Turowski, P.3    Hemmings, B.A.4
  • 37
    • 0029952559 scopus 로고    scopus 로고
    • A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
    • Lee J, Chen Y, Tolstykh T, Stock J. A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain. Proc Natl Acad Sci U S A 1996;93:6043-47
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6043-6047
    • Lee, J.1    Chen, Y.2    Tolstykh, T.3    Stock, J.4
  • 38
    • 0028940016 scopus 로고
    • Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression
    • Turowski P, Fernandez A, Favre B, Lamb NJ, Hemmings BA. Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. J Cell Biol 1995;129:397-410
    • (1995) J Cell Biol , vol.129 , pp. 397-410
    • Turowski, P.1    Fernandez, A.2    Favre, B.3    Lamb, N.J.4    Hemmings, B.A.5
  • 39
    • 0032874184 scopus 로고    scopus 로고
    • Standardization and further development of antigen retrieval immunohistochemistry: Strategies and future goals
    • Shi SR, Cote RJ, Taylor CR. Standardization and further development of antigen retrieval immunohistochemistry: Strategies and future goals. J Histotechnology 1999;22:177-92
    • (1999) J Histotechnology , vol.22 , pp. 177-192
    • Shi, S.R.1    Cote, R.J.2    Taylor, C.R.3
  • 40
    • 0036173980 scopus 로고    scopus 로고
    • Optimization of techniques for the maximal detection and quantification of Alzheimer's-related neuropathology with digital imaging
    • Cummings BJ, Mason AJ, Kim RC, Sheu PC, Anderson AJ. Optimization of techniques for the maximal detection and quantification of Alzheimer's-related neuropathology with digital imaging. Neurobiol Aging 2002;23:161-70
    • (2002) Neurobiol Aging , vol.23 , pp. 161-170
    • Cummings, B.J.1    Mason, A.J.2    Kim, R.C.3    Sheu, P.C.4    Anderson, A.J.5
  • 41
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg SG, Davies P, Schein JD, Binder LI. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J Biol Chem 1992;267:564-69
    • (1992) J Biol Chem , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 42
    • 0035009084 scopus 로고    scopus 로고
    • An overview of common non-Alzheimer dementias
    • Knopman DS. An overview of common non-Alzheimer dementias. Clin Geriatr Med 2001 ;17:281-301
    • (2001) Clin Geriatr Med , vol.17 , pp. 281-301
    • Knopman, D.S.1
  • 43
    • 0036096778 scopus 로고    scopus 로고
    • B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster
    • Li X, Scuderi A, Letsou A, Virshup DM. B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster. Mol Cell Biol 2002;22:3674-84
    • (2002) Mol Cell Biol , vol.22 , pp. 3674-3684
    • Li, X.1    Scuderi, A.2    Letsou, A.3    Virshup, D.M.4
  • 44
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein
    • Eidenmuller J, Path T, Maas T, Pool M, Sontag E, Brandt R. Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. Biochem J 2001;357:759-67
    • (2001) Biochem J , vol.357 , pp. 759-767
    • Eidenmuller, J.1    Path, T.2    Maas, T.3    Pool, M.4    Sontag, E.5    Brandt, R.6
  • 45
    • 0038708285 scopus 로고    scopus 로고
    • Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer's disease
    • Giannakopoulos P Herrmann FR, Bussiere T, Bouras C, Kovari E, Perl DP, et al. Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer's disease. Neurology 2003;60:1495-500
    • (2003) Neurology , vol.60 , pp. 1495-1500
    • Giannakopoulos, P.1    Herrmann, F.R.2    Bussiere, T.3    Bouras, C.4    Kovari, E.5    Perl, D.P.6
  • 46
    • 0034603512 scopus 로고    scopus 로고
    • The role of cerebral ischemia in Alzheimer's disease
    • Kalaria RN. The role of cerebral ischemia in Alzheimer's disease. Neurobiol Aging 2000;21:321-30
    • (2000) Neurobiol Aging , vol.21 , pp. 321-330
    • Kalaria, R.N.1
  • 47
    • 0037103005 scopus 로고    scopus 로고
    • Cerebral post-ischemic reperfusion-induced demethylation of the protein phosphatase 2A catalytic subunit
    • Martin dl V, Burda J, Toledo Lobo MV, Saunas M. Cerebral post-ischemic reperfusion-induced demethylation of the protein phosphatase 2A catalytic subunit. J Neurosci Res 2002;69:540-49
    • (2002) J Neurosci Res , vol.69 , pp. 540-549
    • Martin, D.L.V.1    Burda, J.2    Toledo Lobo, M.V.3    Saunas, M.4
  • 48
    • 0141719852 scopus 로고    scopus 로고
    • Gene-diet interactions in brain aging and neurodegenerative disorders
    • Mattson MP. Gene-diet interactions in brain aging and neurodegenerative disorders. Ann Intern Med 2003;139:441-44
    • (2003) Ann Intern Med , vol.139 , pp. 441-444
    • Mattson, M.P.1
  • 49
    • 0041699719 scopus 로고    scopus 로고
    • Methionine synthase polymorphism is a risk factor for Alzheimer disease
    • Beyer K, Lao JI, Latorre P, et al. Methionine synthase polymorphism is a risk factor for Alzheimer disease. Neuroreport 2003;14:1391-94
    • (2003) Neuroreport , vol.14 , pp. 1391-1394
    • Beyer, K.1    Lao, J.I.2    Latorre, P.3
  • 50
    • 0037042211 scopus 로고    scopus 로고
    • Protein phosphatase 2A methylation: A link between elevated plasma homocysteine and Alzheimer's disease
    • Vafai SB, Stock JB. Protein phosphatase 2A methylation: A link between elevated plasma homocysteine and Alzheimer's disease. FEBS Lett 2002;518:1-4
    • (2002) FEBS Lett , vol.518 , pp. 1-4
    • Vafai, S.B.1    Stock, J.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.