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Volumn 7, Issue MAR, 2014, Pages

Protein phosphatase 2A dysfunction in Alzheimer's disease

Author keywords

Amyloid; Ialzheimer's disease; LCMT1; Methylation; Phosphorylation; Protein phosphatase 2A; Tau

Indexed keywords

AMYLOID; BRAIN PROTEIN; LAMININ ALPHA4; PHOSPHOPROTEIN PHOSPHATASE 2A; TAU PROTEIN;

EID: 84897401611     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00016     Document Type: Article
Times cited : (244)

References (106)
  • 1
    • 33847317020 scopus 로고    scopus 로고
    • Protein kinase A activates protein phosphatase 2A by phosphoryla-tion of the B56delta subunit
    • doi: 10.1073/pnas.0611532104
    • Ahn, J. H., Mcavoy, T., Rakhilin, S. V., Nishi, A., Greengard, P., and Nairn, A. C. (2007). Protein kinase A activates protein phosphatase 2A by phosphoryla-tion of the B56delta subunit. Proc. Natl. Acad. Sci. U.S.A. 104, 2979-2984. doi: 10.1073/pnas.0611532104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 2979-2984
    • Ahn, J.H.1    McAvoy, T.2    Rakhilin, S.V.3    Nishi, A.4    Greengard, P.5    Nairn, A.C.6
  • 2
    • 0031596660 scopus 로고    scopus 로고
    • Phospho-rylation of tau, Abeta-formation, and apoptosis after in vivo inhibition of PP-1 and PP-2A
    • doi: 10.1016/S0197-4580(98)00003-7
    • Arendt, T., Holzer, M., Fruth, R., Bruckner, M. K., and Gartner, U. (1998). Phospho-rylation of tau, Abeta-formation, and apoptosis after in vivo inhibition of PP-1 and PP-2A. Neurobiol.Aging 19, 3-13. doi: 10.1016/S0197-4580(98)00003-7
    • (1998) Neurobiol.Aging , vol.19 , pp. 3-13
    • Arendt, T.1    Holzer, M.2    Fruth, R.3    Bruckner, M.K.4    Gartner, U.5
  • 3
    • 84892941950 scopus 로고    scopus 로고
    • Tau pathology involves protein phosphatase 2A in Parkinsonism-dementia of Guam
    • doi: 10.1073/pnas.1322614111
    • Arif, M., Kazim, S. F., Grundke-Iqbal, I., Garruto, R. M., and Iqbal, K. (2014). Tau pathology involves protein phosphatase 2A in Parkinsonism-dementia of Guam. Proc. Natl. Acad. Sci. U.S.A 111, 1144-1149. doi: 10.1073/pnas.1322614111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 1144-1149
    • Arif, M.1    Kazim, S.F.2    Grundke-Iqbal, I.3    Garruto, R.M.4    Iqbal, K.5
  • 4
    • 34249291912 scopus 로고    scopus 로고
    • Impaired spatial memory in APP-overexpressing mice on a homocysteinemia-inducing diet
    • doi: 10.1016/j.neurobiolaging.2006.05.035
    • Bernardo, A., Mccord, M., Troen, A. M., Allison, J. D., and Mcdon-ald, M. P. (2007). Impaired spatial memory in APP-overexpressing mice on a homocysteinemia-inducing diet. Neurobiol. Aging 28, 1195-1205. doi: 10.1016/j.neurobiolaging.2006.05.035
    • (2007) Neurobiol. Aging , vol.28 , pp. 1195-1205
    • Bernardo, A.1    McCord, M.2    Troen, A.M.3    Allison, J.D.4    McDon-Ald, M.P.5
  • 5
    • 84875628326 scopus 로고    scopus 로고
    • Folate, vitamin B12, and S-adenosylmethionine
    • doi: 10.1016/j.psc.2012.12.001
    • Bottiglieri, T. (2013). Folate, vitamin B12, and S-adenosylmethionine. Psychiatr. Clin. NorthAm. 36,1-13. doi: 10.1016/j.psc.2012.12.001
    • (2013) Psychiatr. Clin. NorthAm , vol.36 , pp. 1-13
    • Bottiglieri, T.1
  • 6
    • 84872062676 scopus 로고    scopus 로고
    • Betaine attenuates Alzheimer-like pathological changes and memory deficits induced by homocysteine
    • doi: 10.1111/jnc.12094
    • Chai, G. S., Jiang, X., Ni, Z. F., Ma, Z.W., Xie, A. J., Cheng, X. S., et al. (2013). Betaine attenuates Alzheimer-like pathological changes and memory deficits induced by homocysteine. J. Neurochem. 124, 388-396. doi: 10.1111/jnc.12094
    • (2013) J. Neurochem , vol.124 , pp. 388-396
    • Chai, G.S.1    Jiang, X.2    Ni, Z.F.3    Ma, Z.W.4    Xie, A.J.5    Cheng, X.S.6
  • 7
    • 0035887601 scopus 로고    scopus 로고
    • An NMDA receptor signaling complex with protein phosphatase 2A
    • Chan, S. F., and Sucher, N. J. (2001). An NMDA receptor signaling complex with protein phosphatase 2A. J. Neurosci. 21, 7985-7992.
    • (2001) J. Neurosci , vol.21 , pp. 7985-7992
    • Chan, S.F.1    Sucher, N.J.2
  • 8
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A bytyrosine phosphorylation
    • doi: 10.1126/science.1325671
    • Chen, J., Martin, B. L., and Brautigan, D. L. (1992). Regulation of protein serine-threonine phosphatase type-2A bytyrosine phosphorylation. Science 257, 1261-1264. doi: 10.1126/science.1325671
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 9
    • 33745370049 scopus 로고    scopus 로고
    • Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine
    • doi: 10.1016/j.febslet.2006.06.021
    • Chohan, M. O., Khatoon, S., Iqbal, I. G., and Iqbal, K. (2006). Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine. FEBS Lett. 580,3973-3979. doi: 10.1016/j.febslet.2006.06.021
    • (2006) FEBS Lett , vol.580 , pp. 3973-3979
    • Chohan, M.O.1    Khatoon, S.2    Iqbal, I.G.3    Iqbal, K.4
  • 10
    • 84862111793 scopus 로고    scopus 로고
    • Folate, homocysteine, vitamin B12, and polymorphisms of genes participating in one-carbon metabolism in late-onset Alzheimer's dis-ease patients and healthy controls
    • doi: 10.1089/ars.2011.4368
    • Coppede, F., Tannorella, P., Pezzini, I., Migheli, F., Ricci, G., Caldarazzo Lenco, E., et al. (2012). Folate, homocysteine, vitamin B12, and polymorphisms of genes participating in one-carbon metabolism in late-onset Alzheimer's dis-ease patients and healthy controls. Antioxid. Redox Signal. 17, 195-204. doi: 10.1089/ars.2011.4368
    • (2012) Antioxid. Redox Signal , vol.17 , pp. 195-204
    • Coppede, F.1    Tannorella, P.2    Pezzini, I.3    Migheli, F.4    Ricci, G.5    Caldarazzo, L.E.6
  • 11
    • 77953892400 scopus 로고    scopus 로고
    • Molecular mechanisms of neurodegeneration in Alzheimer's disease
    • doi: 10.1093/hmg/ddq160
    • Crews, L., and Masliah, E. (2010). Molecular mechanisms of neurodegeneration in Alzheimer's disease. Hum. Mol. Genet. 19, R12-R20. doi: 10.1093/hmg/ddq160
    • (2010) Hum. Mol. Genet , vol.19
    • Crews, L.1    Masliah, E.2
  • 12
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase andcloning of the human homologue
    • doi: 10.1021/bi991646a
    • De Baere, I., Derua, R., Janssens, V., Van Hoof, C., Waelkens, E., Merlevede, W., et al. (1999). Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase andcloning of the human homologue. Biochemistry 38,16539-16547. doi: 10.1021/bi991646a
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • de Baere, I.1    Derua, R.2    Janssens, V.3    van Hoof, C.4    Waelkens, E.5    Merlevede, W.6
  • 13
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphos-phorylated tau protein
    • doi: 10.1042/0264-6021: 3570759
    • Eidenmuller, J., Fath, T., Maas, T., Pool, M., Sontag, E., and Brandt, R. (2001). Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphos-phorylated tau protein. Biochem. J. 357, 759-767. doi: 10.1042/0264-6021: 3570759
    • (2001) Biochem. J , vol.357 , pp. 759-767
    • Eidenmuller, J.1    Fath, T.2    Maas, T.3    Pool, M.4    Sontag, E.5    Brandt, R.6
  • 14
    • 77953300022 scopus 로고    scopus 로고
    • Nuclear export and centrosome targeting of the protein phosphatase 2A subunit B56alpha: Role of B56alpha in nuclear export of the catalytic subunit
    • doi: 10.1074/jbc.M109. 093294
    • Flegg, C. P., Sharma, M., Medina-Palazon, C., Jamieson, C., Galea, M., Bro-cardo, M. G., et al. (2010). Nuclear export and centrosome targeting of the protein phosphatase 2A subunit B56alpha: role of B56alpha in nuclear export of the catalytic subunit. J. Biol. Chem. 285, 18144-18154. doi: 10.1074/jbc.M109. 093294
    • (2010) J. Biol. Chem , vol.285 , pp. 18144-18154
    • Flegg, C.P.1    Sharma, M.2    Medina-Palazon, C.3    Jamieson, C.4    Galea, M.5    Bro-Cardo, M.G.6
  • 15
    • 21744462251 scopus 로고    scopus 로고
    • Homocysteine: Overview ofbiochemistry, molecular biology, and role in disease processes
    • doi: 10.1055/s-2005-872394
    • Fowler, B. (2005). Homocysteine: overview ofbiochemistry, molecular biology, and role in disease processes. Semin. Vasc. Med. 5, 77-86. doi: 10.1055/s-2005-872394
    • (2005) Semin. Vasc. Med , vol.5 , pp. 77-86
    • Fowler, B.1
  • 16
    • 84860368886 scopus 로고    scopus 로고
    • S-adenosylmethionine reduces the progress of the Alzheimer-like features induced byB-vitamin deficiencyin mice
    • doi: 10.1016/j.neurobiolaging.2011.12.013
    • Fuso, A., Nicolia, V., Ricceri, L., Cavallaro, R. A., Isopi, E., Mangia, F., et al. (2012). S-adenosylmethionine reduces the progress of the Alzheimer-like features induced byB-vitamin deficiencyin mice. Neurobiol. Aging 33,1482.e1-1482.e16. doi: 10.1016/j.neurobiolaging.2011.12.013
    • (2012) Neurobiol. Aging , vol.33
    • Fuso, A.1    Nicolia, V.2    Ricceri, L.3    Cavallaro, R.A.4    Isopi, E.5    Mangia, F.6
  • 17
    • 79958766232 scopus 로고    scopus 로고
    • One-carbon metabolism and Alzheimer's dis-ease: Is it all a methylation matter?
    • doi: 10.1016/j.neurobiolaging.2011.01.012
    • Fuso, A., and Scarpa, S. (2011). One-carbon metabolism and Alzheimer's dis-ease: is it all a methylation matter? Neurobiol. Aging 32, 1192-1195. doi: 10.1016/j.neurobiolaging.2011.01.012
    • (2011) Neurobiol. Aging , vol.32 , pp. 1192-1195
    • Fuso, A.1    Scarpa, S.2
  • 18
    • 0033788787 scopus 로고    scopus 로고
    • Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations
    • Goedert, M., Satumtira, S., Jakes, R., Smith, M. J., Kamibayashi, C., White, C. L. III, et al. (2000). Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations. J. Neurochem. 75,2155-2162.
    • (2000) J. Neurochem , vol.75 , pp. 2155-2162
    • Goedert, M.1    Satumtira, S.2    Jakes, R.3    Smith, M.J.4    Kamibayashi, C.5    White III, C.L.6
  • 19
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer disease brain
    • doi: 10.1046/j.1471-4159.1995.65020732.x
    • Gong, C. X., Shaikh, S., Wang, J. Z., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1995). Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 65, 732-738. doi: 10.1046/j.1471-4159.1995.65020732.x
    • (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
  • 20
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • doi: 10.1111/j.1471-4159.1993.tb03603.x
    • Gong, C. X., Singh, T. J., Grundke-Iqbal, I., and Iqbal, K. (1993). Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61, 921-927. doi: 10.1111/j.1471-4159.1993.tb03603.x
    • (1993) J. Neurochem , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 21
    • 80053447207 scopus 로고
    • PP2A targeting by viral proteins: A widespread biological strategy from DNA/RNAtumorvirusesto HIV-1
    • doi: 10.1016/j.bbadis.2011.07.001
    • Guergnon, J., Godet, A. N., Galioot, A., Falanga, P. B., Colle, J. H., Cayla, X., et al. (2011). PP2A targeting by viral proteins: a widespread biological strategy from DNA/RNAtumorvirusesto HIV-1. Biochim. Biophys. Acta 1812,1498-1507. doi: 10.1016/j.bbadis.2011.07.001
    • (1812) Biochim. Biophys. Acta , pp. 1498-1507
    • Guergnon, J.1    Godet, A.N.2    Galioot, A.3    Falanga, P.B.4    Colle, J.H.5    Cayla, X.6
  • 22
    • 0034163509 scopus 로고    scopus 로고
    • Protein phosphatase 2A is associ-ated in an inactive state with microtubules through 2A1-specific interac-tion with tubulin
    • doi: 10.1042/0264-6021: 3460433
    • Hiraga, A., and Tamura, S. (2000). Protein phosphatase 2A is associ-ated in an inactive state with microtubules through 2A1-specific interac-tion with tubulin. Biochem. J. 346(Pt 2), 433-439. doi: 10.1042/0264-6021: 3460433
    • (2000) Biochem. J , vol.346 , Issue.PART 2 , pp. 433-439
    • Hiraga, A.1    Tamura, S.2
  • 23
    • 79960831972 scopus 로고    scopus 로고
    • Association between the MTHFR gene and Alzheimer's disease: A meta-analysis
    • doi: 10.3109/00207454.2011.578778
    • Hua, Y., Zhao, H., Kong, Y., and Ye, M. (2011). Association between the MTHFR gene and Alzheimer's disease: a meta-analysis. Int. J. Neurosci. 121, 462-471. doi: 10.3109/00207454.2011.578778
    • (2011) Int. J. Neurosci , vol.121 , pp. 462-471
    • Hua, Y.1    Zhao, H.2    Kong, Y.3    Ye, M.4
  • 24
    • 39949083195 scopus 로고    scopus 로고
    • PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
    • doi: 10.1016/j.tibs.2007.12.004
    • Janssens, V., Longin, S., and Goris, J. (2008). PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail). Trends Biochem. Sci. 33, 113-121. doi: 10.1016/j.tibs.2007.12.004
    • (2008) Trends Biochem. Sci , vol.33 , pp. 113-121
    • Janssens, V.1    Longin, S.2    Goris, J.3
  • 25
    • 84878863522 scopus 로고    scopus 로고
    • Okadaic acid induced neurotoxicity: An emerging tool to study Alzheimer's disease pathology
    • doi: 10.1016/j.neuro.2013.05.002
    • Kamat, P. K., Rai, S., and Nath, C. (2013). Okadaic acid induced neurotoxicity: an emerging tool to study Alzheimer's disease pathology. Neurotoxicology 37, 163-172. doi: 10.1016/j.neuro.2013.05.002
    • (2013) Neurotoxicology , vol.37 , pp. 163-172
    • Kamat, P.K.1    Rai, S.2    Nath, C.3
  • 26
    • 0025895035 scopus 로고
    • Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit
    • Kamibayashi, C., Estes, R., Slaughter, C., and Mumby, M. C. (1991). Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit. J. Biol. Chem. 266, 13251-13260.
    • (1991) J. Biol. Chem , vol.266 , pp. 13251-13260
    • Kamibayashi, C.1    Estes, R.2    Slaughter, C.3    Mumby, M.C.4
  • 27
    • 78650746798 scopus 로고    scopus 로고
    • Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling
    • doi: 10.1073/pnas.0912793107
    • Kickstein, E., Krauss, S., Thornhill, P., Rutschow, D., Zeller, R., Sharkey, J., et al. (2010). Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling. Proc. Natl. Acad. Sci. U.S.A. 107,21830-21835. doi: 10.1073/pnas.0912793107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 21830-21835
    • Kickstein, E.1    Krauss, S.2    Thornhill, P.3    Rutschow, D.4    Zeller, R.5    Sharkey, J.6
  • 28
    • 84875179717 scopus 로고    scopus 로고
    • Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites
    • doi: 10.1074/jbc.M112.433326
    • Kimura, T., Tsutsumi, K., Taoka, M., Saito, T., Masuda-Suzukake, M., Ishiguro, K., et al. (2013). Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites. J. Biol. Chem. 288, 7968-7977. doi: 10.1074/jbc.M112.433326
    • (2013) J. Biol. Chem , vol.288 , pp. 7968-7977
    • Kimura, T.1    Tsutsumi, K.2    Taoka, M.3    Saito, T.4    Masuda-Suzukake, M.5    Ishiguro, K.6
  • 29
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activityinduces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • doi: 10.1074/jbc.M102621200
    • Kins, S., Crameri, A., Evans, D. R., Hemmings, B. A., Nitsch, R. M., and Gotz, J. (2001). Reduced protein phosphatase 2A activityinduces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276, 38193-38200. doi: 10.1074/jbc.M102621200
    • (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
  • 30
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • doi: 10.1016/S0002-9440(10) 63444-X
    • Kins, S., Kurosinski, P., Nitsch, R. M., and Gotz, J. (2003). Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am. J. Pathol. 163, 833-843. doi: 10.1016/S0002-9440(10) 63444-X
    • (2003) Am. J. Pathol , vol.163 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Gotz, J.4
  • 31
    • 84891719063 scopus 로고    scopus 로고
    • Protein phosphatase 2A is regulated by protein kinase calpha (PKCalpha)-dependent phosphorylation of its targeting subunit B56alpha at Ser41
    • doi: 10.1074/jbc.M113.507996
    • Kirchhefer, U., Heinick, A., Konig, S., Kristensen, T., Muller, F. U., Seidl, M. D., et al. (2014). Protein phosphatase 2A is regulated by protein kinase calpha (PKCalpha)-dependent phosphorylation of its targeting subunit B56alpha at Ser41. J. Biol. Chem. 289, 163-176. doi: 10.1074/jbc.M113.507996
    • (2014) J. Biol. Chem , vol.289 , pp. 163-176
    • Kirchhefer, U.1    Heinick, A.2    Konig, S.3    Kristensen, T.4    Muller, F.U.5    Seidl, M.D.6
  • 32
    • 84897410573 scopus 로고    scopus 로고
    • PR65A phosphorylation regulates PP2A complex signaling
    • doi: 10.1371/journal.pone.0085000
    • Kotlo, K., Xing, Y., Lather, S., Grillon, J. M., Johnson, K., Skidgel, R. A., et al. (2014). PR65A phosphorylation regulates PP2A complex signaling. PLoS ONE 9:e85000. doi: 10.1371/journal.pone.0085000
    • (2014) PLoS ONE , vol.9
    • Kotlo, K.1    Xing, Y.2    Lather, S.3    Grillon, J.M.4    Johnson, K.5    Skidgel, R.A.6
  • 33
    • 0036523032 scopus 로고    scopus 로고
    • Folic acid deficiency and homocysteine impair DNA repair in hippocampal neurons and sensitize them to amyloid toxicity in experimental models of Alzheimer's disease
    • Kruman, L.L., Kumaravel, T. S., Lohani, A., Pedersen, W. A., Cutler, R. G., Kruman, Y., et al. (2002). Folic acid deficiency and homocysteine impair DNA repair in hippocampal neurons and sensitize them to amyloid toxicity in experimental models of Alzheimer's disease. J. Neurosci. 22, 1752-1762.
    • (2002) J. Neurosci , vol.22 , pp. 1752-1762
    • Kruman, L.L.1    Kumaravel, T.S.2    Lohani, A.3    Pedersen, W.A.4    Cutler, R.G.5    Kruman, Y.6
  • 34
    • 79959534777 scopus 로고    scopus 로고
    • Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau
    • doi: 10.1371/journal.pone.0021521
    • Landrieu, I., Smet-Nocca, C., Amniai, L., Louis, J. V., Wieruszeski, J. M., Goris, J., et al. (2011). Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau. PLoS ONE 6:e21521. doi: 10.1371/journal.pone.0021521
    • (2011) PLoS ONE , vol.6
    • Landrieu, I.1    Smet-Nocca, C.2    Amniai, L.3    Louis, J.V.4    Wieruszeski, J.M.5    Goris, J.6
  • 35
    • 10944228450 scopus 로고    scopus 로고
    • Tau and src family tyrosine kinases
    • doi: 10.1016/j.bbadis.2004.09.002
    • Lee, G. (2005). Tau and src family tyrosine kinases. Biochim. Biophys. Acta 1739, 323-330. doi: 10.1016/j.bbadis.2004.09.002
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 323-330
    • Lee, G.1
  • 36
    • 0029952559 scopus 로고    scopus 로고
    • A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
    • doi: 10.1073/pnas.93. 12.6043
    • Lee, J., Chen, Y., Tolstykh, T., and Stock, J. (1996). A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain. Proc. Natl. Acad. Sci. U.S.A. 93, 6043-6047. doi: 10.1073/pnas.93. 12.6043
    • (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
  • 37
    • 35648957688 scopus 로고    scopus 로고
    • Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells
    • doi: 10.1074/jbc.M704861200
    • Lee, J. A., and Pallas, D. C. (2007). Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells. J. Biol. Chem. 282, 30974-30984. doi: 10.1074/jbc.M704861200
    • (2007) J. Biol. Chem , vol.282 , pp. 30974-30984
    • Lee, J.A.1    Pallas, D.C.2
  • 38
    • 10744229024 scopus 로고    scopus 로고
    • Structure of protein phosphatase methyltrans-ferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity
    • doi: 10.1074/jbc.M311484200
    • Leulliot, N., Quevillon-Cheruel, S., Sorel, I., Li De La Sierra-Gallay, I., Collinet, B., Graille, M., et al. (2004). Structure of protein phosphatase methyltrans-ferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity. J. Biol. Chem. 279, 8351-8358. doi: 10.1074/jbc.M311484200
    • (2004) J. Biol. Chem , vol.279 , pp. 8351-8358
    • Leulliot, N.1    Quevillon-Cheruel, S.2    Sorel, I.3    Li De La Sierra-Gallay, I.4    Collinet, B.5    Graille, M.6
  • 39
    • 0031603730 scopus 로고    scopus 로고
    • I1PP2A and I2PP2A. Two potent protein phosphatase 2A-specific inhibitor proteins
    • doi: 10.1385/0-89603-468-2:59
    • Li, M., and Damuni, Z. (1998). I1PP2A and I2PP2A. Two potent protein phosphatase 2A-specific inhibitor proteins. Methods Mol. Biol. 93, 59-66. doi: 10.1385/0-89603-468-2:59
    • (1998) Methods Mol. Biol , vol.93 , pp. 59-66
    • Li, M.1    Damuni, Z.2
  • 40
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • doi: 10.1111/j.1460-9568.2005.04391.x
    • Liu, F., Grundke-Iqbal, I., Iqbal, K., and Gong, C. X. (2005). Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci. 22, 1942-1950. doi: 10.1111/j.1460-9568.2005.04391.x
    • (2005) Eur. J. Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 41
    • 47049089041 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase-3 inhibits protein phosphatase-2A and the underlying mechanisms
    • doi: 10.1016/j.neurobiolaging.2007.03.012
    • Liu, G. P., Zhang, Y., Yao, X. Q., Zhang, C. E., Fang, J., Wang, Q., et al. (2008a). Activation of glycogen synthase kinase-3 inhibits protein phosphatase-2A and the underlying mechanisms. Neurobiol. Aging 29, 1348-1358. doi: 10.1016/j.neurobiolaging.2007.03.012
    • (2008) Neurobiol. Aging , vol.29 , pp. 1348-1358
    • Liu, G.P.1    Zhang, Y.2    Yao, X.Q.3    Zhang, C.E.4    Fang, J.5    Wang, Q.6
  • 42
    • 41149086325 scopus 로고    scopus 로고
    • Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibril-lary pathology
    • doi: 10.1111/j.1582-4934.2008.00249.x
    • Liu, R., Zhou, X.W., Tanila, H., Bjorkdahl, C., Wang, J.Z., Guan, Z.Z., et al. (2008b). Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibril-lary pathology. J. Cell. Mol. Med. 12, 241-257. doi: 10.1111/j.1582-4934.2008. 00249.x
    • (2008) J. Cell. Mol. Med , vol.12 , pp. 241-257
    • Liu, R.1    Zhou, X.W.2    Tanila, H.3    Bjorkdahl, C.4    Wang, J.Z.5    Guan, Z.Z.6
  • 43
    • 36549071636 scopus 로고    scopus 로고
    • Spatial control of protein phosphatase 2A (de)methylation
    • doi: 10.1016/j.yexcr.2007.07.030
    • Longin, S., Zwaenepoel, K., Martens, E., Louis, J. V., Rondelez, E., Goris, J., et al. (2008). Spatial control of protein phosphatase 2A (de)methylation. Exp. Cell Res. 314, 68-81. doi: 10.1016/j.yexcr.2007.07.030
    • (2008) Exp. Cell Res , vol.314 , pp. 68-81
    • Longin, S.1    Zwaenepoel, K.2    Martens, E.3    Louis, J.V.4    Rondelez, E.5    Goris, J.6
  • 44
    • 84903704713 scopus 로고    scopus 로고
    • Plasma nutrient status of patients with Alzheimer's disease: Systematic review and meta-analysis
    • doi: 10.1016/j.jalz.2013.05.1771 [Epub ahead of print]
    • Lopes da Silva, S., Vellas, B., Elemans, S., Luchsinger, J., Kamphuis, P., Yaffe, K., et al. (2013). Plasma nutrient status of patients with Alzheimer's disease: systematic review and meta-analysis. Alzheimers Dement doi: 10.1016/j.jalz.2013.05.1771 [Epub ahead of print].
    • (2013) Alzheimers Dement
    • Lopes da Silva, S.1    Vellas, B.2    Elemans, S.3    Luchsinger, J.4    Kamphuis, P.5    Yaffe, K.6
  • 45
    • 0035692472 scopus 로고    scopus 로고
    • A gene expression profile of Alzheimer's disease
    • doi: 10.1089/10445490152717541
    • Loring, J. F., Wen, X., Lee, J. M., Seilhamer, J., and Somogyi, R. (2001). A gene expression profile of Alzheimer's disease. DNA Cell Biol. 20, 683-695. doi: 10.1089/10445490152717541
    • (2001) DNA Cell Biol , vol.20 , pp. 683-695
    • Loring, J.F.1    Wen, X.2    Lee, J.M.3    Seilhamer, J.4    Somogyi, R.5
  • 46
    • 79955566269 scopus 로고    scopus 로고
    • Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta
    • doi: 10.1073/pnas.1018 777108
    • Louis, J. V., Martens, E., Borghgraef, P., Lambrecht, C., Sents, W., Lon-gin, S., et al. (2011). Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta. Proc. Natl. Acad. Sci. U.S.A. 108, 6957-6962. doi: 10.1073/pnas.1018 777108
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 6957-6962
    • Louis, J.V.1    Martens, E.2    Borghgraef, P.3    Lambrecht, C.4    Sents, W.5    Lon-Gin, S.6
  • 47
    • 84875245784 scopus 로고    scopus 로고
    • PTPA activates protein phosphatase-2A through reducing its phos-phorylation at tyrosine-307 with upregulation of protein tyrosine phosphatase 1B
    • doi: 10.1016/j.bbamcr.2013. 02.005
    • Luo, Y., Nie, Y. J., Shi, H. R., Ni, Z. F., Wang, Q., Wang, J. Z., et al. (2013). PTPA activates protein phosphatase-2A through reducing its phos-phorylation at tyrosine-307 with upregulation of protein tyrosine phosphatase 1B. Biochim. Biophys. Acta 1833, 1235-1243. doi: 10.1016/j.bbamcr.2013. 02.005
    • (2013) Biochim. Biophys. Acta , pp. 1235-1243
    • Luo, Y.1    Nie, Y.J.2    Shi, H.R.3    Ni, Z.F.4    Wang, Q.5    Wang, J.Z.6
  • 48
    • 84879261109 scopus 로고    scopus 로고
    • Circumventing embryonic lethality with Lcmt1 deficiency: Generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signaling
    • doi: 10.1371/journal.pone.0065967
    • MacKay, K. B., Tu, Y., Young, S. G., and Clarke, S. G. (2013). Circumventing embryonic lethality with Lcmt1 deficiency: generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signaling. PLoS ONE 8:e65967. doi: 10.1371/journal.pone. 0065967
    • (2013) PLoS ONE , vol.8
    • Mackay, K.B.1    Tu, Y.2    Young, S.G.3    Clarke, S.G.4
  • 49
    • 0031004401 scopus 로고    scopus 로고
    • Protein phosphatase inhibitors induce modification of synapse structure and tau hyperphosphorylation in cultured rat hippocampal neurons
    • doi: 10.1002/(SICI)1097-4547(19970601)48:5<425::AID-JNR4>3.0.C0;2-G
    • Malchiodi-Albedi, F., Petrucci, T. C., Picconi, B., Iosi, F., and Falchi, M. (1997). Protein phosphatase inhibitors induce modification of synapse structure and tau hyperphosphorylation in cultured rat hippocampal neurons. J. Neurosci. Res. 48, 425-438. doi: 10.1002/(SICI)1097-4547(19970601)48:5<425::AID-JNR4>3.0.C0;2-G
    • (1997) J. Neurosci. Res , vol.48 , pp. 425-438
    • Malchiodi-Albedi, F.1    Petrucci, T.C.2    Picconi, B.3    Iosi, F.4    Falchi, M.5
  • 50
    • 84887627010 scopus 로고    scopus 로고
    • Association of methylenetetrahydrofolate reductase polymorphisms with susceptibility to Alzheimer's disease
    • doi: 10.1016/j.clineuro.2013.03.015
    • Mansouri, L., Fekih-Mrissa, N., Klai, S., Mansour, M., Gritli, N., and Mrissa, R. (2013). Association of methylenetetrahydrofolate reductase polymorphisms with susceptibility to Alzheimer's disease. Clin. Neurol. Neurosurg. 115, 1693-1696. doi: 10.1016/j.clineuro.2013.03.015
    • (2013) Clin. Neurol. Neurosurg , vol.115 , pp. 1693-1696
    • Mansouri, L.1    Fekih-Mrissa, N.2    Klai, S.3    Mansour, M.4    Gritli, N.5    Mrissa, R.6
  • 51
    • 14944350207 scopus 로고    scopus 로고
    • Role of protein phosphatase 2A in mGluR5-regulated MEK/ERK phosphorylation in neurons
    • doi: 10.1074/jbc.M411709200
    • Mao, L., Yang, L., Arora, A., Choe, E. S., Zhang, G., Liu, Z., et al. (2005). Role of protein phosphatase 2A in mGluR5-regulated MEK/ERK phosphorylation in neurons. J. Biol. Chem. 280,12602-12610. doi: 10.1074/jbc.M411709200
    • (2005) J. Biol. Chem , vol.280 , pp. 12602-12610
    • Mao, L.1    Yang, L.2    Arora, A.3    Choe, E.S.4    Zhang, G.5    Liu, Z.6
  • 52
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimer's disease
    • doi: 10.1016/j.neuint.2010.12.023
    • Martin, L., Latypova, X., and Terro, F. (2011). Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem. Int. 58, 458-471. doi: 10.1016/j.neuint.2010.12.023
    • (2011) Neurochem. Int , vol.58 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 53
    • 77749298896 scopus 로고    scopus 로고
    • Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination
    • doi: 10.1021/bi901837h
    • McConnell, J. L., Watkins, G. R., Soss, S. E., Franz, H. S., Mccorvey, L. R., Spiller, B.W., et al. (2010). Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination. Biochemistry 49, 1713-1718. doi: 10.1021/bi901837h
    • (2010) Biochemistry , vol.49 , pp. 1713-1718
    • McConnell, J.L.1    Watkins, G.R.2    Soss, S.E.3    Franz, H.S.4    McCorvey, L.R.5    Spiller, B.W.6
  • 54
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • doi: 10.1074/jbc.271.36.22081
    • McCright, B., Rivers, A. M., Audlin, S., and Virshup, D. M. (1996). The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J. Biol. Chem. 271,22081-22089. doi: 10.1074/jbc.271.36.22081
    • (1996) J. Biol. Chem , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 55
    • 84876902735 scopus 로고    scopus 로고
    • Understanding the relationship between GSK-3 and Alzheimers disease: A focus on how GSK-3 can modulate synaptic plasticity processes
    • doi: 10.1586/ern.13.39
    • Medina, M., and Avila, J. (2013). Understanding the relationship between GSK-3 and Alzheimers disease: a focus on how GSK-3 can modulate synaptic plasticity processes. Expert Rev. Neurother. 13, 495-503. doi: 10.1586/ern.13.39
    • (2013) Expert Rev. Neurother , vol.13 , pp. 495-503
    • Medina, M.1    Avila, J.2
  • 56
    • 84890392083 scopus 로고    scopus 로고
    • New insights into the role of glycogen syn-thase kinase-3 in Alzheimers disease
    • doi: 10.1517/14728222.2013.843670
    • Medina, M., and Avila, J. (2014). New insights into the role of glycogen syn-thase kinase-3 in Alzheimers disease. Expert Opin. Ther. Targets 18, 69-77. doi: 10.1517/14728222.2013.843670
    • (2014) Expert Opin. Ther. Targets , vol.18 , pp. 69-77
    • Medina, M.1    Avila, J.2
  • 57
    • 84875329449 scopus 로고    scopus 로고
    • The role of B vitamins in preventing and treating cog-nitive impairment and decline
    • doi: 10.3945/an.112.002535
    • Morris, M. S. (2012). The role of B vitamins in preventing and treating cog-nitive impairment and decline. Adv. Nutr. 3, 801-812. doi: 10.3945/an.112. 002535
    • (2012) Adv. Nutr , vol.3 , pp. 801-812
    • Morris, M.S.1
  • 58
    • 77957910119 scopus 로고    scopus 로고
    • Dementia revealed: Novel chromosome 6 locus for late-onset Alzheimer disease provides genetic evidence for folate-pathway abnormalities
    • doi: 10.1371/journal.pgen.1001130
    • Naj, A. C., Beecham, G. W., Martin, E. R., Gallins, P. J., Powell, E. H., Konidari, I., et-al. (2010). Dementia revealed: novel chromosome 6 locus for late-onset Alzheimer disease provides genetic evidence for folate-pathway abnormalities. PLoS Genet. 6:e1001130. doi: 10.1371/journal.pgen.1001130
    • (2010) PLoS Genet , vol.6
    • Naj, A.C.1    Beecham, G.W.2    Martin, E.R.3    Gallins, P.J.4    Powell, E.H.5    Konidari, I.6
  • 59
    • 77149130504 scopus 로고    scopus 로고
    • B vitamin deficiency promotes tau phosphorylation through regulation of GSK3beta and PP2A
    • doi: 10.3233/JAD-2010-1284
    • Nicolia, V., Fuso, A., Cavallaro, R. A., Di Luzio, A., and Scarpa, S. (2010). B vitamin deficiency promotes tau phosphorylation through regulation of GSK3beta and PP2A. J. AlzheimersDis. 19, 895-907. doi: 10.3233/JAD-2010-1284.
    • (2010) J. AlzheimersDis , vol.19 , pp. 895-907
    • Nicolia, V.1    Fuso, A.2    Cavallaro, R.A.3    Di Luzio, A.4    Scarpa, S.5
  • 60
    • 34247625153 scopus 로고    scopus 로고
    • Expression of protein phosphatase 2A mutants and silencing of the regulatory B alpha subunit induce a selective loss of acetylated and detyrosinated microtubules
    • doi: 10.1111/j.1471-4159.2007.04503.x
    • Nunbhakdi-Craig, V., Schuechner, S., Sontag, J. M., Montgomery, L., Pallas, D. C., Juno, C., et al. (2007). Expression of protein phosphatase 2A mutants and silencing of the regulatory B alpha subunit induce a selective loss of acetylated and detyrosinated microtubules. J. Neurochem. 101, 959-971. doi: 10.1111/j.1471-4159.2007.04503.x
    • (2007) J. Neurochem , vol.101 , pp. 959-971
    • Nunbhakdi-Craig, V.1    Schuechner, S.2    Sontag, J.M.3    Montgomery, L.4    Pallas, D.C.5    Juno, C.6
  • 61
    • 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
    • doi: 10.1074/jbc.274.20.14382
    • Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., et al. (1999). 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. 274,14382-14391. doi: 10.1074/jbc.274.20.14382
    • (1999) J. Biol. Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6
  • 62
    • 33744788667 scopus 로고    scopus 로고
    • Hyperhomocysteinemic Alzheimer's mouse model of amyloidosis shows increased brain amyloid beta peptide levels
    • doi: 10.1016/j.nbd.2006.01.005
    • Pacheco-Quinto, J., Rodriguez De Turco, E. B., Derosa, S., Howard, A., Cruz-Sanchez, F., Sambamurti, K., et al. (2006). Hyperhomocysteinemic Alzheimer's mouse model of amyloidosis shows increased brain amyloid beta peptide levels. Neurobiol. Dis. 22, 651-656. doi: 10.1016/j.nbd.2006.01.005
    • (2006) Neurobiol. Dis , vol.22 , pp. 651-656
    • Pacheco-Quinto, J.1    Rodriguez De Turco, E.B.2    Derosa, S.3    Howard, A.4    Cruz-Sanchez, F.5    Sambamurti, K.6
  • 63
    • 0031435589 scopus 로고    scopus 로고
    • Elevated protein levels of protein phosphatases PP-2A and PP-2B in astrocytes of Alzheimer's disease temporal cortex
    • doi: 10.1007/BF01294734
    • Pei, J. J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., and Cowburn, R. F. (1997). Elevated protein levels of protein phosphatases PP-2A and PP-2B in astrocytes of Alzheimer's disease temporal cortex. J. Neural Transm. 104, 1329-1338. doi: 10.1007/BF01294734
    • (1997) J. Neural Transm , vol.104 , pp. 1329-1338
    • Pei, J.J.1    Grundke-Iqbal, I.2    Iqbal, K.3    Bogdanovic, N.4    Winblad, B.5    Cowburn, R.F.6
  • 64
    • 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
    • doi: 10.1074/jbc.M102780200
    • Planel, E., Yasutake, K., Fujita, S. C., and Ishiguro, K. (2001). 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. 276, 34298-34306. doi: 10.1074/jbc.M102780200
    • (2001) J. Biol. Chem , vol.276 , pp. 34298-34306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 65
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • doi: 10.1074/jbc.M603469200
    • Plattner, F., Angelo, M., and Giese, K. P. (2006). The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 281, 25457-25465. doi: 10.1074/jbc.M603469200
    • (2006) J. Biol. Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 66
    • 84876360474 scopus 로고    scopus 로고
    • Hyperhomocysteinemic mice show cognitive impairment without features of Alzheimer's disease phenotype
    • doi: 10.3233/JAD-122347
    • Rhodehouse, B. C., Erickson, M. A., Banks, W. A., and Bearden, S. E. (2013). Hyperhomocysteinemic mice show cognitive impairment without features of Alzheimer's disease phenotype. J. Alzheimers Dis. 35, 59-66. doi: 10.3233/JAD-122347.
    • (2013) J. Alzheimers Dis , vol.35 , pp. 59-66
    • Rhodehouse, B.C.1    Erickson, M.A.2    Banks, W.A.3    Bearden, S.E.4
  • 67
    • 33646476174 scopus 로고    scopus 로고
    • Altered phosphorylation of cytoskelet al proteins in mutant protein phosphatase 2A transgenic mice
    • doi: 10.1016/j.bbrc.2006.03.066
    • Schild, A., Ittner, L. M., and Gotz, J. (2006).Altered phosphorylation of cytoskelet al proteins in mutant protein phosphatase 2A transgenic mice. Biochem. Biophys. Res. Commun. 343, 1171-1178. doi: 10.1016/j.bbrc.2006.03.066
    • (2006) Biochem. Biophys. Res. Commun , vol.343 , pp. 1171-1178
    • Schild, A.1    Ittner, L.M.2    Gotz, J.3
  • 68
    • 78649409678 scopus 로고    scopus 로고
    • B vitamins and the aging brain
    • doi: 10.1111/j.1753-4887.2010.00346.x
    • Selhub, J., Troen, A., and Rosenberg, I. H. (2010). B vitamins and the aging brain. Nutr. Rev. 68(Suppl. 2), S112-S118. doi: 10.1111/j.1753-4887.2010.00346.x
    • (2010) Nutr. Rev , vol.68 , Issue.SUPPL. 2
    • Selhub, J.1    Troen, A.2    Rosenberg, I.H.3
  • 69
    • 84872761033 scopus 로고    scopus 로고
    • The biogenesis of active protein phosphatase 2A holoenzymes: A tightly reg-ulated process creating phosphatase specificity
    • doi: 10.1111/j.1742-4658.2012.08579.x
    • Sents, W., Ivanova, E., Lambrecht, C., Haesen, D., and Janssens, V. (2013). The biogenesis of active protein phosphatase 2A holoenzymes: a tightly reg-ulated process creating phosphatase specificity. FEBS J. 280, 644-661. doi: 10.1111/j.1742-4658.2012.08579.x
    • (2013) FEBS J , vol.280 , pp. 644-661
    • Sents, W.1    Ivanova, E.2    Lambrecht, C.3    Haesen, D.4    Janssens, V.5
  • 70
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • doi: 10.1016/S0898-6568(00)00123-6
    • Sontag, E. (2001). Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell. Signal. 13, 7-16. doi: 10.1016/S0898-6568(00)00123-6
    • (2001) Cell. Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 71
    • 5644293035 scopus 로고    scopus 로고
    • Downregulation of protein phosphatase 2A carboxyl methyla-tion and methyltransferase may contribute to Alzheimer disease pathogenesis
    • Sontag, E., Hladik, C., Montgomery, L., Luangpirom, A., Mudrak, I., Ogris, E., et al. (2004a). Downregulation of protein phosphatase 2A carboxyl methyla-tion and methyltransferase may contribute to Alzheimer disease pathogenesis. J. Neuropathol. Exp. Neurol. 63, 1080-1091.
    • (2004) J. Neuropathol. Exp. Neurol , vol.63 , pp. 1080-1091
    • Sontag, E.1    Hladik, C.2    Montgomery, L.3    Luangpirom, A.4    Mudrak, I.5    Ogris, E.6
  • 72
    • 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., Mudrak, I., Ogris, E., Speciale, S., et al. (2004b). Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology. J. Neuropathol. Exp. Neurol. 63,287-301.
    • (2004) J. Neuropathol. Exp. Neurol , vol.63 , pp. 287-301
    • Sontag, E.1    Luangpirom, A.2    Hladik, C.3    Mudrak, I.4    Ogris, E.5    Speciale, S.6
  • 73
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • doi: 10.1083/jcb.128.6.1131
    • Sontag, E., Nunbhakdi-Craig, V., Bloom, G. S., and Mumby, M. C. (1995). A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol. 128, 1131-1144. doi: 10.1083/jcb.128.6.1131
    • (1995) J. Cell Biol , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 74
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A
    • doi: 10.1016/S0896-6273(00)80250-0
    • Sontag, E., Nunbhakdi-Craig, V., Lee, G., Bloom, G. S., and Mumby, M. C. (1996). Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron 17, 1201-1207. doi: 10.1016/S0896-6273(00)80250-0
    • (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
  • 75
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies
    • doi: 10.1074/jbc.274.36.25490
    • Sontag, E., Nunbhakdi-Craig, V., Lee, G., Brandt, R., Kamibayashi, C., Kuret, J., et al. (1999). Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies. J. Biol. Chem. 274, 25490-25498. doi: 10.1074/jbc.274.36.25490
    • (1999) J. Biol. Chem , vol.274 , pp. 25490-25498
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Brandt, R.4    Kamibayashi, C.5    Kuret, J.6
  • 76
    • 33947328858 scopus 로고    scopus 로고
    • Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation
    • doi: 10.1523/JNEUROSCI.3316-06.2007
    • Sontag, E., Nunbhakdi-Craig, V., Sontag, J. M., Diaz-Arrastia, R., Ogris, E., Dayal, S., et al. (2007). Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation. J. Neurosci. 27, 2751-2759. doi: 10.1523/JNEUROSCI.3316-06.2007
    • (2007) J. Neurosci , vol.27 , pp. 2751-2759
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Sontag, J.M.3    Diaz-Arrastia, R.4    Ogris, E.5    Dayal, S.6
  • 77
    • 78649984662 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A methylation byLCMT1 and PME-1 plays a critical role in differentiation of neuroblastoma cells
    • doi: 10.1111/j.1471-4159.2010.07049.x
    • Sontag, J. M., Nunbhakdi-Craig, V., Mitterhuber, M., Ogris, E., and Sontag, E. (2010). Regulation of protein phosphatase 2A methylation byLCMT1 and PME-1 plays a critical role in differentiation of neuroblastoma cells. J. Neurochem. 115, 1455-1465. doi: 10.1111/j.1471-4159.2010.07049.x
    • (2010) J. Neurochem , vol.115 , pp. 1455-1465
    • Sontag, J.M.1    Nunbhakdi-Craig, V.2    Mitterhuber, M.3    Ogris, E.4    Sontag, E.5
  • 78
    • 58149213742 scopus 로고    scopus 로고
    • Folate deficiency induces in vitro and mouse brain region-specific downregulation of leucine carboxyl methyltransferase-1 and protein phosphatase 2A B(alpha) subunit expression that correlate with enhanced tau phosphorylation
    • doi: 10.1523/JNEUROSCI.2816-08.2008
    • Sontag, J. M., Nunbhakdi-Craig, V., Montgomery, L., Arning, E., Bottiglieri, T., and Sontag, E. (2008). Folate deficiency induces in vitro and mouse brain region-specific downregulation of leucine carboxyl methyltransferase-1 and protein phosphatase 2A B(alpha) subunit expression that correlate with enhanced tau phosphorylation. J. Neurosci. 28, 11477-11487. doi: 10.1523/JNEUROSCI.2816-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 11477-11487
    • Sontag, J.M.1    Nunbhakdi-Craig, V.2    Montgomery, L.3    Arning, E.4    Bottiglieri, T.5    Sontag, E.6
  • 79
    • 84884537540 scopus 로고    scopus 로고
    • Leucine carboxyl methyltransferase 1 (LCMT1)-dependent methylation regulates the associa-tion of protein phosphatase 2A and Tau protein with plasma membrane microdomains in neuroblastoma cells
    • doi: 10.1074/jbc.M113.490102
    • Sontag, J. M., Nunbhakdi-Craig, V., and Sontag, E. (2013). Leucine carboxyl methyltransferase 1 (LCMT1)-dependent methylation regulates the associa-tion of protein phosphatase 2A and Tau protein with plasma membrane microdomains in neuroblastoma cells. J. Biol. Chem. 288, 27396-27405. doi: 10.1074/jbc.M113.490102
    • (2013) J. Biol. Chem , vol.288 , pp. 27396-27405
    • Sontag, J.M.1    Nunbhakdi-Craig, V.2    Sontag, E.3
  • 80
    • 84860354271 scopus 로고    scopus 로고
    • The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: Implications for tauopathies
    • doi: 10.1074/jbc.M111.338681
    • Sontag, J. M., Nunbhakdi-Craig, V., White, C. L. III, Halpain, S., and Sontag, E. (2012). The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: implications for tauopathies. J. Biol. Chem. 287, 14984-14993. doi: 10.1074/jbc.M111.338681
    • (2012) J. Biol. Chem , vol.287 , pp. 14984-14993
    • Sontag, J.M.1    Nunbhakdi-Craig, V.2    White, C.L.III.3    Halpain, S.4    Sontag, E.5
  • 81
    • 79956098248 scopus 로고    scopus 로고
    • Toward defining the preclinical stages of Alzheimer's disease: Recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease
    • doi: 10.1016/j.jalz.2011.03.003
    • Sperling, R. A., Aisen, P. S., Beckett, L. A., Bennett, D. A., Craft, S., Fagan, A. M., et al. (2011). Toward defining the preclinical stages of Alzheimer's disease: recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease. Alzheimers Dement 7, 280-292. doi: 10.1016/j.jalz.2011.03.003
    • (2011) Alzheimers Dement , vol.7 , pp. 280-292
    • Sperling, R.A.1    Aisen, P.S.2    Beckett, L.A.3    Bennett, D.A.4    Craft, S.5    Fagan, A.M.6
  • 83
    • 0032536810 scopus 로고    scopus 로고
    • Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits
    • doi: 10.1002/(SICI)1096-9861(19980323)392:4<515::AID-CNE8>3.0. CO;2-3
    • Strack, S., Zaucha, J. A., Ebner, F. F., Colbran, R. J., and Wadzinski, B. E. (1998). Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits. J. Comp. Neurol. 392, 515-527. doi: 10.1002/(SICI)1096-9861(19980323)392:4<515::AID-CNE8>3.0. CO;2-3
    • (1998) J. Comp. Neurol , vol.392 , pp. 515-527
    • Strack, S.1    Zaucha, J.A.2    Ebner, F.F.3    Colbran, R.J.4    Wadzinski, B.E.5
  • 84
    • 0037728833 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A-and protein phosphatase 1-induced tau hyperphos-phorylation and impairment of spatial memory retention in rats
    • doi: 10.1016/S0306-4522(02)00697-8
    • Sun, L., Liu, S.Y., Zhou, X.W., Wang, X. C., Liu, R., Wang, Q., et al. (2003). Inhibition of protein phosphatase 2A-and protein phosphatase 1-induced tau hyperphos-phorylation and impairment of spatial memory retention in rats. Neuroscience 118, 1175-1182. doi: 10.1016/S0306-4522(02)00697-8
    • (2003) Neuroscience , vol.118 , pp. 1175-1182
    • Sun, L.1    Liu, S.Y.2    Zhou, X.W.3    Wang, X.C.4    Liu, R.5    Wang, Q.6
  • 85
    • 34447275978 scopus 로고    scopus 로고
    • Small-molecule inhibitors ofser/thr protein phosphatases: Specificity, use and common forms of abuse
    • doi: 10.1385/1-59745-267-X:23
    • Swingle, M., Ni, L., and Honkanen, R.E. (2007). Small-molecule inhibitors ofser/thr protein phosphatases: specificity, use and common forms of abuse. Methods Mol. Biol. 365,23-38. doi: 10.1385/1-59745-267-X:23
    • (2007) Methods Mol. Biol , vol.365 , pp. 23-38
    • Swingle, M.1    Ni, L.2    Honkanen, R.E.3
  • 86
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A inAlzheimer's disease
    • doi: 10.1016/S0002-9440(10)62486-8
    • Tanimukai, H., Grundke-Iqbal, I., and Iqbal, K. (2005). Up-regulation of inhibitors of protein phosphatase-2A inAlzheimer's disease. Am. J. Pathol. 166, 1761-1771. doi: 10.1016/S0002-9440(10)62486-8
    • (2005) Am. J. Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 87
    • 77956385203 scopus 로고    scopus 로고
    • Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models
    • doi: 10.1073/pnas.1009038107
    • van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Gotz, J., et al. (2010). Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models. Proc. Natl. Acad. Sci. U.S.A. 107, 13888-13893. doi: 10.1073/pnas.1009038107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 13888-13893
    • van Eersel, J.1    Ke, Y.D.2    Liu, X.3    Delerue, F.4    Kril, J.J.5    Gotz, J.6
  • 88
    • 61649127812 scopus 로고    scopus 로고
    • From promiscuity to preci-sion: Protein phosphatases get a makeover
    • doi: 10.1016/j.molcel.2009.02.015
    • Virshup, D. M., and Shenolikar, S. (2009). From promiscuity to preci-sion: protein phosphatases get a makeover. Mol. Cell 33, 537-545. doi: 10.1016/j.molcel.2009.02.015
    • (2009) Mol. Cell , vol.33 , pp. 537-545
    • Virshup, D.M.1    Shenolikar, S.2
  • 89
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • doi: 10.1006/exnr.20 01.7630
    • Vogelsberg-Ragaglia, V., Schuck, T., Trojanowski, J. Q., and Lee, V. M. (2001). PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp. Neurol. 168, 402-412. doi: 10.1006/exnr.20 01.7630
    • (2001) Exp. Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 90
    • 79958744416 scopus 로고    scopus 로고
    • Phosphoprotein phos-phatase 2A: A novel druggable target for Alzheimer's disease
    • doi: 10.4155/fmc.11.47
    • Voronkov, M., Braithwaite, S. P., and Stock, J. B. (2011). Phosphoprotein phos-phatase 2A: a novel druggable target for Alzheimer's disease. Future Med. Chem. 3, 821-833. doi: 10.4155/fmc.11.47
    • (2011) Future Med. Chem , vol.3 , pp. 821-833
    • Voronkov, M.1    Braithwaite, S.P.2    Stock, J.B.3
  • 91
    • 49949108971 scopus 로고    scopus 로고
    • Age-specific epigenetic drift in late-onset Alzheimer's disease
    • doi: 10.1371/jour-nal.pone.0002698
    • Wang, S. C., Oelze, B., and Schumacher, A. (2008). Age-specific epigenetic drift in late-onset Alzheimer's disease. PLoS ONE 3:e2698. doi: 10.1371/jour-nal.pone.0002698
    • (2008) PLoS ONE , vol.3
    • Wang, S.C.1    Oelze, B.2    Schumacher, A.3
  • 92
    • 78649859760 scopus 로고    scopus 로고
    • The carboxy-terminal fragment of inhibitor-2 of protein phosphatase-2A induces Alzheimer disease pathology and cognitive impairment
    • doi: 10.1096/fj.10-158477
    • Wang, X., Blanchard, J., Kohlbrenner, E., Clement, N., Linden, R. M., Radu, A., et al. (2010). The carboxy-terminal fragment of inhibitor-2 of protein phosphatase-2A induces Alzheimer disease pathology and cognitive impairment. FASEB J. 24, 4420-4432. doi: 10.1096/fj.10-158477
    • (2010) FASEB J , vol.24 , pp. 4420-4432
    • Wang, X.1    Blanchard, J.2    Kohlbrenner, E.3    Clement, N.4    Linden, R.M.5    Radu, A.6
  • 93
    • 84863788681 scopus 로고    scopus 로고
    • Monoubiquitination promotes cal-pain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phos-phorylation
    • doi: 10.1074/jbc.M112.368613
    • Watkins, G. R., Wang, N., Mazalouskas, M. D., Gomez, R. J., Guthrie, C.R., Kraemer, B. C., et al. (2012). Monoubiquitination promotes cal-pain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phos-phorylation. J. Biol. Chem. 287, 24207-24215. doi: 10.1074/jbc.M112. 368613
    • (2012) J. Biol. Chem , vol.287 , pp. 24207-24215
    • Watkins, G.R.1    Wang, N.2    Mazalouskas, M.D.3    Gomez, R.J.4    Guthrie, C.R.5    Kraemer, B.C.6
  • 94
    • 82555195174 scopus 로고    scopus 로고
    • Folate/vitamin-B12 prevents chronic hyperhomocysteinemia-induced tau hyper-phosphorylation and memory deficits in aged rats
    • doi: 10.3233/JAD-2011-110770
    • Wei, W., Liu, Y. H., Zhang, C. E., Wang, Q., Wei, Z., Mousseau, D. D., et al. (2011). Folate/vitamin-B12 prevents chronic hyperhomocysteinemia-induced tau hyper-phosphorylation and memory deficits in aged rats. J.AlzheimersDis. 27, 639-650. doi: 10.3233/JAD-2011-110770.
    • (2011) J.AlzheimersDis , vol.27 , pp. 639-650
    • Wei, W.1    Liu, Y.H.2    Zhang, C.E.3    Wang, Q.4    Wei, Z.5    Mousseau, D.D.6
  • 95
    • 57749176350 scopus 로고    scopus 로고
    • Peroxynitrite-dependent activation of protein phosphatase type 2A mediates microvascular endothelial barrier dysfunction
    • doi: 10.1093/cvr/cvn246
    • Wu, F., and Wilson, J. X. (2009). Peroxynitrite-dependent activation of protein phosphatase type 2A mediates microvascular endothelial barrier dysfunction. Cardiovasc. Res. 81, 38-45. doi: 10.1093/cvr/cvn246
    • (2009) Cardiovasc. Res , vol.81 , pp. 38-45
    • Wu, F.1    Wilson, J.X.2
  • 96
    • 41149175685 scopus 로고    scopus 로고
    • Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    • doi: 10.1016/j.cell.2008.02.041
    • Xing, Y., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., and Shi, Y. (2008). Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell 133, 154-163. doi: 10.1016/j.cell.2008.02.041
    • (2008) Cell , vol.133 , pp. 154-163
    • Xing, Y.1    Li, Z.2    Chen, Y.3    Stock, J.B.4    Jeffrey, P.D.5    Shi, Y.6
  • 97
    • 84870481575 scopus 로고    scopus 로고
    • Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phospho-rylation
    • doi: 10.1016/j.neurobiolaging.2012. 07.003
    • Xiong, Y., Jing, X. P., Zhou, X. W., Wang, X. L., Yang, Y., Sun, X. Y., et al. (2013). Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phospho-rylation. Neurobiol. Aging 34, 745-756. doi: 10.1016/j.neurobiolaging.2012. 07.003
    • (2013) Neurobiol. Aging , vol.34 , pp. 745-756
    • Xiong, Y.1    Jing, X.P.2    Zhou, X.W.3    Wang, X.L.4    Yang, Y.5    Sun, X.Y.6
  • 98
    • 52049100425 scopus 로고    scopus 로고
    • Struc-ture of a protein phosphatase 2A holoenzyme: Insights into B55-mediated Tau dephosphorylation
    • doi: 10.1016/j.molcel.2008.08.006
    • Xu, Y., Chen, Y., Zhang, P., Jeffrey, P. D., and Shi, Y. (2008). Struc-ture of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation. Mol. Cell 31, 873-885. doi: 10.1016/j.molcel.2008. 08.006
    • (2008) Mol. Cell , vol.31 , pp. 873-885
    • Xu, Y.1    Chen, Y.2    Zhang, P.3    Jeffrey, P.D.4    Shi, Y.5
  • 99
    • 84864289760 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates leucine-309 demethylation of pro-tein phosphatase-2A via PPMT1 and PME-1
    • doi: 10.1016/j.febslet.2012.06.018
    • Yao, X. Q., Li, X. C., Zhang, X. X., Yin, Y. Y., Liu, B., Luo, D. J., et al. (2012). Glycogen synthase kinase-3beta regulates leucine-309 demethylation of pro-tein phosphatase-2A via PPMT1 and PME-1. FEBS Lett. 586, 2522-2528. doi: 10.1016/j.febslet.2012.06.018
    • (2012) FEBS Lett , vol.586 , pp. 2522-2528
    • Yao, X.Q.1    Li, X.C.2    Zhang, X.X.3    Yin, Y.Y.4    Liu, B.5    Luo, D.J.6
  • 100
    • 79959736543 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates Tyr307 phosphorylation of protein phosphatase-2A via protein tyrosine phosphatase 1B but not Src
    • doi: 10.1042/BJ20110347
    • Yao, X. Q., Zhang, X. X., Yin, Y. Y., Liu, B., Luo, D. J., Liu, D., et al. (2011). Glycogen synthase kinase-3beta regulates Tyr307 phosphorylation of protein phosphatase-2A via protein tyrosine phosphatase 1B but not Src. Biochem. J. 437, 335-344. doi: 10.1042/BJ20110347
    • (2011) Biochem. J , vol.437 , pp. 335-344
    • Yao, X.Q.1    Zhang, X.X.2    Yin, Y.Y.3    Liu, B.4    Luo, D.J.5    Liu, D.6
  • 101
    • 51649119364 scopus 로고    scopus 로고
    • Homocysteine induces tau phosphorylation by inactivating protein phosphatase 2A in rat hippocampus
    • doi: 10.1016/j.neurobiolaging.2007.04.015
    • Zhang, C. E., Tian, Q., Wei, W., Peng, J. H., Liu, G. P., Zhou, X. W., et al. (2008) Homocysteine induces tau phosphorylation by inactivating protein phosphatase 2A in rat hippocampus. Neurobiol. Aging 29, 1654-1665. doi: 10.1016/j.neurobiolaging.2007.04.015
    • (2008) Neurobiol. Aging , vol.29 , pp. 1654-1665
    • Zhang, C.E.1    Tian, Q.2    Wei, W.3    Peng, J.H.4    Liu, G.P.5    Zhou, X.W.6
  • 102
    • 65349162724 scopus 로고    scopus 로고
    • Hyperhomocysteinemia increases beta-amyloid by enhancing expres-sion of gamma-secretase and phosphorylation of amyloid precursor protein in rat brain
    • doi: 10.2353/ajpath.2009.081036
    • Zhang, C. E., Wei, W., Liu, Y. H., Peng, J. H., Tian, Q., Liu, G. P., et al. (2009). Hyperhomocysteinemia increases beta-amyloid by enhancing expres-sion of gamma-secretase and phosphorylation of amyloid precursor protein in rat brain. Am. J. Pathol. 174, 1481-1491. doi: 10.2353/ajpath.2009. 081036
    • (2009) Am. J. Pathol , vol.174 , pp. 1481-1491
    • Zhang, C.E.1    Wei, W.2    Liu, Y.H.3    Peng, J.H.4    Tian, Q.5    Liu, G.P.6
  • 103
    • 0030991668 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae homologs of mammalian B and B' sub-units of protein phosphatase 2A direct the enzyme to distinct cellu-lar functions
    • doi: 10.1074/jbc.272.13.8256
    • Zhao, Y., Boguslawski, G., Zitomer, R. S., and Depaoli-Roach, A. A. (1997). Saccharomyces cerevisiae homologs of mammalian B and B' sub-units of protein phosphatase 2A direct the enzyme to distinct cellu-lar functions. J. Biol. Chem. 272, 8256-8262. doi: 10.1074/jbc.272. 13.8256
    • (1997) J. Biol. Chem , vol.272 , pp. 8256-8262
    • Zhao, Y.1    Boguslawski, G.2    Zitomer, R.S.3    Depaoli-Roach, A.A.4
  • 104
    • 77949675424 scopus 로고    scopus 로고
    • Diet-induced hyperhomocysteinemia increases amyloid-beta formation and deposition in a mouse model of Alzheimer's disease
    • doi: 10.2174/156720510790691326
    • Zhuo, J. M., Portugal, G. S., Kruger, W. D., Wang, H., Gould, T. J., and Pratico, D. (2010). Diet-induced hyperhomocysteinemia increases amyloid-beta formation and deposition in a mouse model of Alzheimer's disease. Curr. Alzheimer Res. 7, 140-149. doi: 10.2174/156720510790691326
    • (2010) Curr. Alzheimer Res , vol.7 , pp. 140-149
    • Zhuo, J.M.1    Portugal, G.S.2    Kruger, W.D.3    Wang, H.4    Gould, T.J.5    Pratico, D.6
  • 105
    • 76749128435 scopus 로고    scopus 로고
    • Acceleration of brain amyloidosis in an Alzheimer's disease mouse model by a folate, vitamin B6 and B12-deficient diet
    • doi: 10.1016/j.exger.2009.12.005
    • Zhuo, J. M., and Pratico, D. (2010). Acceleration of brain amyloidosis in an Alzheimer's disease mouse model by a folate, vitamin B6 and B12-deficient diet. Exp. Gerontol. 45, 195-201. doi: 10.1016/j.exger.2009.12.005
    • (2010) Exp. Gerontol , vol.45 , pp. 195-201
    • Zhuo, J.M.1    Pratico, D.2
  • 106
    • 80052024330 scopus 로고    scopus 로고
    • Is hyperhomocysteinemia an Alzheimer's disease (AD) risk factor, an AD marker, or neither?
    • doi: 10.1016/j.tips.2011.05.003
    • Zhuo, J. M., Wang, H., and Pratico, D. (2011). Is hyperhomocysteinemia an Alzheimer's disease (AD) risk factor, an AD marker, or neither? Trends Pharmacol. Sci. 32,562-571. doi: 10.1016/j.tips.2011.05.003
    • (2011) Trends Pharmacol. Sci , vol.32 , pp. 562-571
    • Zhuo, J.M.1    Wang, H.2    Pratico, D.3


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