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Volumn 11, Issue 10, 2015, Pages 1803-1820

GBA deficiency promotes SNCA/α-synuclein accumulation through autophagic inhibition by inactivated PPP2A

Author keywords

Autophagy; Glucocerebrosidase; Parkinson disease; Protein phosphatase 2A; synuclein

Indexed keywords

ALPHA SYNUCLEIN; AUTOPHAGY PROTEIN 5; BAFILOMYCIN A1; BECLIN 1; CERAMIDE; GLUCOSYLCERAMIDASE; MESSENGER RNA; PHOSPHOPROTEIN PHOSPHATASE 2A; RAPAMYCIN; SHORT HAIRPIN RNA; PHOSPHOPROTEIN PHOSPHATASE 2; PPP2CA PROTEIN, HUMAN; PPP2CA PROTEIN, MOUSE; PPP2CA PROTEIN, RAT; SNCA PROTEIN, HUMAN; SNCA PROTEIN, MOUSE; SNCA PROTEIN, RAT;

EID: 84953856105     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2015.1086055     Document Type: Article
Times cited : (106)

References (56)
  • 1
    • 37349004102 scopus 로고    scopus 로고
    • Parkinson disease
    • Spec No. Two, PMID:17911161
    • Thomas B, Beal MF. Parkinson disease. Hum Mol Genet 2007; 16 Spec No. Two:R183-94; PMID:17911161; http://dx.doi.org/10.1093/hmg/ddm159
    • (2007) Hum Mol Genet , vol.16
    • Thomas, B.1    Beal, M.F.2
  • 2
    • 80055082804 scopus 로고    scopus 로고
    • Parkinson disease and a-synuclein expression
    • PMID:21887711
    • Devine MJ, Gwinn K, Singleton A, Hardy J. Parkinson disease and a-synuclein expression. Mov Disord 2011; 26:2160-8; PMID:21887711; http://dx.doi.org/10.1002/mds.23948
    • (2011) Mov Disord , vol.26 , pp. 2160-2168
    • Devine, M.J.1    Gwinn, K.2    Singleton, A.3    Hardy, J.4
  • 3
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson disease: From monogenic forms to genetic susceptibility factors
    • PMID:19297401
    • Lesage S, Brice A. Parkinson disease: from monogenic forms to genetic susceptibility factors. Hum Mol Genet 2009; 18:R48-59; PMID:19297401; http://dx.doi.org/10.1093/hmg/ddp012
    • (2009) Hum Mol Genet , vol.18
    • Lesage, S.1    Brice, A.2
  • 7
    • 79956324138 scopus 로고    scopus 로고
    • Large-scale screening of the Gaucher’s disease-related glucocerebrosidase gene in Europeans with Parkinson disease
    • PMID:20947659
    • Lesage S, Anheim M, Condroyer C, Pollak P, Durif F, Dupuits C, Viallet F, Lohmann E, Corvol JC, Honore A, et al. Large-scale screening of the Gaucher’s disease-related glucocerebrosidase gene in Europeans with Parkinson disease. Hum MolGenet 2011; 20:202-10; PMID:20947659; http://dx.doi.org/10.1093/hmg/ddq454
    • (2011) Hum Molgenet , vol.20 , pp. 202-210
    • Lesage, S.1    Anheim, M.2    Condroyer, C.3    Pollak, P.4    Durif, F.5    Dupuits, C.6    Viallet, F.7    Lohmann, E.8    Corvol, J.C.9    Honore, A.10
  • 8
    • 0038465682 scopus 로고
    • The Metabolism of Glucocerebrosides. I. Purification and Properties of a Glucocerebroside-Cleaving Enzyme from Spleen Tissue
    • PMID:14253443
    • Brady RO, Kanfer J, Shapiro D. The Metabolism of Glucocerebrosides. I. Purification and Properties of a Glucocerebroside-Cleaving Enzyme from Spleen Tissue. J Biol Chem 1965; 240:39-43; PMID:14253443
    • (1965) J Biol Chem , vol.240 , pp. 39-43
    • Brady, R.O.1    Kanfer, J.2    Shapiro, D.3
  • 9
    • 42949118684 scopus 로고    scopus 로고
    • Gaucher disease: Mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA)
    • PMID:18338393
    • Hruska KS, LaMarca ME, Scott CR, Sidransky E. Gaucher disease: mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA). Hum Mutat 2008; 29:567-83; PMID:18338393; http://dx. doi.org/10.1002/humu.20676
    • (2008) Hum Mutat , vol.29 , pp. 567-583
    • Hruska, K.S.1    Lamarca, M.E.2    Scott, C.R.3    Sidransky, E.4
  • 10
    • 33646837867 scopus 로고    scopus 로고
    • Increased incidence of Parkinson disease among relatives of patients with Gaucher disease
    • PMID:16651014
    • Halperin A, Elstein D, Zimran A. Increased incidence of Parkinson disease among relatives of patients with Gaucher disease. Blood Cells Mol Dis 2006; 36:426-8; PMID:16651014; http://dx.doi.org/10.1016/j.bcmd. 2006.02.004
    • (2006) Blood Cells Mol Dis , vol.36 , pp. 426-428
    • Halperin, A.1    Elstein, D.2    Zimran, A.3
  • 11
    • 34548726339 scopus 로고    scopus 로고
    • Mutations in the glucocerebrosidase gene are associated with early-onset Parkinson disease
    • PMID:17875915
    • Clark LN, Ross BM, Wang Y, Mejia-Santana H, Harris J, Louis ED, Cote LJ, Andrews H, Fahn S, Waters C, et al. Mutations in the glucocerebrosidase gene are associated with early-onset Parkinson disease. Neurology 2007; 69:1270-7; PMID:17875915; http://dx.doi.org/10.1212/01.wnl.0000276989.17578.02
    • (2007) Neurology , vol.69 , pp. 1270-1277
    • Clark, L.N.1    Ross, B.M.2    Wang, Y.3    Mejia-Santana, H.4    Harris, J.5    Louis, E.D.6    Cote, L.J.7    Rews, H.8    Fahn, S.9    Waters, C.10
  • 15
    • 84867036900 scopus 로고    scopus 로고
    • Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains
    • PMID:23034917
    • Gegg ME, Burke D, Heales SJ, Cooper JM, Hardy J, Wood NW, Schapira AH. Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains. Ann Neurol 2012; 72:455-63; PMID:23034917; http://dx.doi.org/10.1002/ana.23614
    • (2012) Ann Neurol , vol.72 , pp. 455-463
    • Gegg, M.E.1    Burke, D.2    Heales, S.J.3    Cooper, J.M.4    Hardy, J.5    Wood, N.W.6    Schapira, A.H.7
  • 16
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and a-synuclein form a bidirectional pathogenic loop in synucleinopathies
    • PMID:21700325
    • Mazzulli JR, Xu YH, Sun Y, Knight AL, McLean PJ, Caldwell GA, Sidransky E, Grabowski GA, Krainc D. Gaucher disease glucocerebrosidase and a-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 2011; 146:37-52; PMID:21700325; http://dx.doi.org/10.1016/j.cell.2011.06.001
    • (2011) Cell , vol.146 , pp. 37-52
    • Mazzulli, J.R.1    Xu, Y.H.2    Sun, Y.3    Knight, A.L.4    McLean, P.J.5    Caldwell, G.A.6    Sidransky, E.7    Grabowski, G.A.8    Krainc, D.9
  • 17
    • 79956199921 scopus 로고    scopus 로고
    • Saftig P,Woulfe J, et al. Acid b-glucosidase mutants linked to Gaucher disease, Parkinson disease, and Lewy body dementia alter a-synuclein processing
    • PMID:21472771
    • Cullen V, Sardi SP, Ng J, Xu YH, Sun Y, Tomlinson JJ, Kolodziej P, Kahn I, Saftig P,Woulfe J, et al. Acid b-glucosidase mutants linked to Gaucher disease, Parkinson disease, and Lewy body dementia alter a-synuclein processing. Ann Neurol 2011; 69:940-53; PMID:21472771; http://dx.doi.org/10.1002/ana.22400
    • (2011) Ann Neurol , vol.69 , pp. 940-953
    • Cullen, V.1    Sardi, S.P.2    Ng, J.3    Xu, Y.H.4    Sun, Y.5    Tomlinson, J.J.6    Kolodziej, P.7    Kahn, I.8
  • 18
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in a-synuclein models of Parkinson and Lewy body diseases
    • PMID:19864570
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, Adame A, Wyss-Coray T, Masliah E. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in a-synuclein models of Parkinson and Lewy body diseases. J Neurosci 2009; 29:13578-88; PMID:19864570; http://dx.doi.org/10.1523/JNEUROSCI.4390-09.2009
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 19
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • Chen J,Martin BL, Brautigan DL, PMID:1325671
    • Chen J,Martin BL, Brautigan DL. Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science 1992; 257:1261-4; PMID:1325671; http://dx.doi.org/10.1126/science.1325671
    • (1992) Science , vol.257 , pp. 1261-1264
  • 20
    • 84859398214 scopus 로고    scopus 로고
    • Synemin promotes AKT-dependent glioblastoma cell proliferation by antagonizing PP2A
    • PMID:22337773
    • Pitre A, Davis N, Paul M, Orr AW, Skalli O. Synemin promotes AKT-dependent glioblastoma cell proliferation by antagonizing PP2A. Mol Biol Cell 2012; 23:1243-53; PMID:22337773; http://dx.doi.org/10.1091/mbc.E11-08-0685
    • (2012) Mol Biol Cell , vol.23 , pp. 1243-1253
    • Pitre, A.1    Davis, N.2    Paul, M.3    Orr, A.W.4    Skalli, O.5
  • 21
    • 84862501584 scopus 로고    scopus 로고
    • Carnosic acid modulates Akt/IKK/NF-kappaB signaling by PP2A and induces intrinsic and extrinsic pathway mediated apoptosis in human prostate carcinoma PC-3 cells
    • PMID:22453599
    • Kar S, Palit S, Ball WB, Das PK. Carnosic acid modulates Akt/IKK/NF-kappaB signaling by PP2A and induces intrinsic and extrinsic pathway mediated apoptosis in human prostate carcinoma PC-3 cells. Apoptosis 2012; 17:735-47; PMID:22453599; http://dx.doi.org/10.1007/s10495-012-0715-4
    • (2012) Apoptosis , vol.17 , pp. 735-747
    • Kar, S.1    Palit, S.2    Ball, W.B.3    Das, P.K.4
  • 22
    • 84867399176 scopus 로고    scopus 로고
    • DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3beta to downregulate b-catenin transcription target, osteopontin
    • PMID:22266849
    • Mitra A, Menezes ME, Pannell LK, Mulekar MS, Honkanen RE, Shevde LA, Samant RS. DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3beta to downregulate b-catenin transcription target, osteopontin. Oncogene 2012; 31:4472-83; PMID:22266849; http://dx.doi.org/101038/onc.2011.623
    • (2012) Oncogene , vol.31 , pp. 4472-4483
    • Mitra, A.1    Menezes, M.E.2    Pannell, L.K.3    Mulekar, M.S.4    Honkanen, R.E.5    Shevde, L.A.6    Samant, R.S.7
  • 23
    • 67650237693 scopus 로고    scopus 로고
    • Tap42- associated protein phosphatase type 2A negatively regulates induction of autophagy
    • PMID:19223769
    • Yorimitsu T, He C, Wang K, Klionsky DJ. Tap42- associated protein phosphatase type 2A negatively regulates induction of autophagy. Autophagy 2009; 5:616-24; PMID:19223769; http://dx.doi.org/104161/auto.5.5.8091
    • (2009) Autophagy , vol.5 , pp. 616-624
    • Yorimitsu, T.1    He, C.2    Wang, K.3    Klionsky, D.J.4
  • 25
    • 33745859721 scopus 로고    scopus 로고
    • Autophagy, bafilomycin and cell death: The “a-B-cs" of plecomacrolideinduced neuroprotection
    • PMID:16874105
    • Shacka JJ, Klocke BJ, Roth KA. Autophagy, bafilomycin and cell death: the “a-B-cs" of plecomacrolideinduced neuroprotection. Autophagy 2006; 2:228-30; PMID:16874105; http://dx.doi.org/104161/auto.2703
    • (2006) Autophagy , vol.2 , pp. 228-230
    • Shacka, J.J.1    Klocke, B.J.2    Roth, K.A.3
  • 26
    • 2442485884 scopus 로고    scopus 로고
    • Ceramidemediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1
    • PMID:14970205
    • Scarlatti F, Bauvy C, Ventruti A, Sala G, Cluzeaud F, Vandewalle A, Ghidoni R, Codogno P. Ceramidemediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1. J Biol Chem 2004; 279:18384-91; PMID:14970205; http://dx.doi.org/10.1074/jbc.M313561200
    • (2004) J Biol Chem , vol.279 , pp. 18384-18391
    • Scarlatti, F.1    Bauvy, C.2    Ventruti, A.3    Sala, G.4    Cluzeaud, F.5    Vandewalle, A.6    Ghidoni, R.7    Codogno, P.8
  • 27
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • PMID:20153326
    • Komatsu M, Ichimura Y. Physiological significance of selective degradation of p62 by autophagy. FEBS Lett 2010; 584:1374-8; PMID:20153326; http://dx.doi. org/10.1016/j.febslet.2010.02.017
    • (2010) FEBS Lett , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 28
    • 33947328858 scopus 로고    scopus 로고
    • Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation
    • PMID:17360897
    • Sontag E, Nunbhakdi-Craig V, Sontag JM, Diaz-Arrastia R, Ogris E, Dayal S, Lentz SR, Arning E, Bottiglieri T. Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation. J Neurosci 2007; 27:2751-9; PMID:17360897; http://dx.doi.org/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    Lentz, S.R.7    Arning, E.8    Bottiglieri, T.9
  • 29
    • 84869014351 scopus 로고    scopus 로고
    • Disruption of protein quality control in Parkinson disease
    • PMID:22553500
    • Cook C, Stetler C, Petrucelli L. Disruption of protein quality control in Parkinson disease. Cold Spring Harb Perspect Med 2012; 2:a009423; PMID:22553500; http://dx.doi.org/10.1101/cshperspect.a009423
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Cook, C.1    Stetler, C.2    Petrucelli, L.3
  • 30
    • 38949096081 scopus 로고    scopus 로고
    • Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome
    • PMID:17986870
    • Ding WX, Yin XM. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 2008; 4:141-50; PMID:17986870; http://dx.doi.org/10.4161/auto.5190
    • (2008) Autophagy , vol.4 , pp. 141-150
    • Ding, W.X.1    Yin, X.M.2
  • 32
    • 36949031267 scopus 로고    scopus 로고
    • α-Synucleinopathy models and human neuropathology: Similarities and differences
    • PMID:17932682
    • Kahle PJ. α-Synucleinopathy models and human neuropathology: similarities and differences. Acta Neuropathol 2008; 115:87-95; PMID:17932682; http://dx.doi.org/10.1007/s00401-007-0302-x
    • (2008) Acta Neuropathol , vol.115 , pp. 87-95
    • Kahle, P.J.1
  • 33
    • 84875967929 scopus 로고    scopus 로고
    • Loss of b-glucocerebrosidase activity does not affect a-synuclein levels or lysosomal function in neuronal cells
    • PMID:23580063
    • Dermentzaki G, Dimitriou E, Xilouri M, Michelakakis H, Stefanis L. Loss of b-glucocerebrosidase activity does not affect a-synuclein levels or lysosomal function in neuronal cells. PLoS One 2013; 8:e60674; PMID:23580063; http://dx.doi.org/10.1371/journal. pone.0060674
    • (2013) Plos One , vol.8
    • Dermentzaki, G.1    Dimitriou, E.2    Xilouri, M.3    Michelakakis, H.4    Stefanis, L.5
  • 34
    • 84861595545 scopus 로고    scopus 로고
    • Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of a-synuclein and LRRK2 in the brain
    • PMID:22649237
    • Friedman LG, Lachenmayer ML, Wang J, He L, Poulose SM, Komatsu M, Holstein GR, Yue Z. Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of a-synuclein and LRRK2 in the brain. J Neurosci 2012; 32:7585-93; PMID:22649237; http://dx.doi.org/10.1523/JNEUROSCI.5809-11.2012
    • (2012) J Neurosci , vol.32 , pp. 7585-7593
    • Friedman, L.G.1    Lachenmayer, M.L.2    Wang, J.3    He, L.4    Poulose, S.M.5    Komatsu, M.6    Holstein, G.R.7    Yue, Z.8
  • 37
    • 76349098949 scopus 로고    scopus 로고
    • Crosstalk between apoptosis and autophagy within the Beclin 1 interactome
    • PMID:20125189
    • Maiuri MC, Criollo A, Kroemer G. Crosstalk between apoptosis and autophagy within the Beclin 1 interactome. EMBO J 2010; 29:515-6; PMID:20125189; http://dx.doi.org/10.1038/emboj.2009.377
    • (2010) EMBO J , vol.29 , pp. 515-516
    • Maiuri, M.C.1    Criollo, A.2    Kroemer, G.3
  • 38
    • 84894528843 scopus 로고    scopus 로고
    • Reduced glucocerebrosidase is associated with increased a-synuclein in sporadic Parkinson disease
    • PMID:24477431
    • Murphy KE, Gysbers AM, Abbott SK, Tayebi N, Kim WS, Sidransky E, Cooper A, Garner B, Halliday GM. Reduced glucocerebrosidase is associated with increased a-synuclein in sporadic Parkinson disease. Brain 2014; 137:834-48; PMID:24477431; http://dx.doi.org/10.1093/brain/awt367
    • (2014) Brain , vol.137 , pp. 834-848
    • Murphy, K.E.1    Gysbers, A.M.2    Abbott, S.K.3    Tayebi, N.4    Kim, W.S.5    Sidransky, E.6    Cooper, A.7    Garner, B.8    Halliday, G.M.9
  • 39
    • 80052640576 scopus 로고    scopus 로고
    • Declining phosphatases underlie aging-related hyperphosphorylation of neurofilaments
    • PMID:20031277
    • Veeranna Yang DS, Lee JH, Vinod KY, Stavrides P, Amin ND, Pant HC, Nixon RA. Declining phosphatases underlie aging-related hyperphosphorylation of neurofilaments. Neurobiol Aging 2011; 32:2016-29; PMID:20031277; http://dx.doi.org/10.1016/j.neurobiolaging.2009.12.001
    • (2011) Neurobiol Aging , vol.32 , pp. 2016-2029
    • Veeranna Yang, D.S.1    Lee, J.H.2    Vinod, K.Y.3    Stavrides, P.4    Amin, N.D.5    Pant, H.C.6    Nixon, R.A.7
  • 41
    • 0037151038 scopus 로고    scopus 로고
    • A functional role for the B56 a-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function
    • PMID:11929874
    • Ruvolo PP, Clark W, Mumby M, Gao F, May WS. A functional role for the B56 a-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function. J Biol Chem 2002; 277:22847-52; PMID:11929874; http://dx.doi.org/10.1074/jbc.M201830200
    • (2002) J Biol Chem , vol.277 , pp. 22847-22852
    • Ruvolo, P.P.1    Clark, W.2    Mumby, M.3    Gao, F.4    May, W.S.5
  • 42
    • 0032520898 scopus 로고    scopus 로고
    • Bipotential roles of ceramide in the growth of hippocampal neurons: Promotion of cell survival and dendritic outgrowth in dose- and developmental stage-dependent manners
    • PMID:9545085
    • Mitoma J, Ito M, Furuya S, Hirabayashi Y. Bipotential roles of ceramide in the growth of hippocampal neurons: promotion of cell survival and dendritic outgrowth in dose- and developmental stage-dependent manners. J Neurosci Res 1998; 51:712-22;PMID:9545085;http://dx.doi.org/10.1002/(SICI)1097-4547(19980315)51:6%3c712:AIDJNR5%3e3.0.CO;2-E
    • (1998) J Neurosci Res , vol.51 , pp. 712-722
    • Mitoma, J.1    Ito, M.2    Furuya, S.3    Hirabayashi, Y.4
  • 43
    • 11844273281 scopus 로고    scopus 로고
    • Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau
    • PMID:15642345
    • Tsujio I, Zaidi T, Xu J, Kotula L, Grundke-Iqbal I, Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau. FEBS Lett 2005; 579:363-72; PMID:15642345; http://dx.doi.org/10.1016/j.febslet.2004.11.097
    • (2005) FEBS Lett , vol.579 , pp. 363-372
    • Tsujio, I.1    Zaidi, T.2    Xu, J.3    Kotula, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 44
    • 44849144122 scopus 로고    scopus 로고
    • I1PP2A affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A
    • PMID:18245083
    • Chen S, Li B, Grundke-Iqbal I, Iqbal K. I1PP2A affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A. J Biol Chem 2008; 283:10513-21; PMID:18245083; http://dx.doi.org/10.1074/jbc.M709852200
    • (2008) J Biol Chem , vol.283 , pp. 10513-10521
    • Chen, S.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 45
    • 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
    • PMID:11160832
    • Yu XX, Du X, Moreno CS, Green RE, Ogris E, Feng Q, Chou L, McQuoid MJ, Pallas DC. 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; PMID:11160832; http://dx.doi.org/10.1091/mbc.12.1.185
    • (2001) Mol Biol Cell , vol.12 , pp. 185-199
    • Yu, X.X.1    Du, X.2    Moreno, C.S.3    Green, R.E.4    Ogris, E.5    Feng, Q.6    Chou, L.7    McQuoid, M.J.8    Pallas, D.C.9
  • 46
    • 39949083195 scopus 로고    scopus 로고
    • PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
    • PMID:18291659
    • Janssens V, Longin S, Goris J. PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail). Trends Biochem Sci 2008; 33:113-21; PMID:18291659; http://dx.doi.org/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
  • 47
    • 5644293035 scopus 로고    scopus 로고
    • Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis
    • PMID:15535135
    • Sontag E, Hladik C, Montgomery L, Luangpirom A, Mudrak I, Ogris E, White CL, 3rd. Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J Neuropathol Exp Neurol 2004; 63:1080-91; PMID:15535135
    • (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    White, C.L.7
  • 48
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology
    • PMID: 15099019
    • Sontag E, Luangpirom A, Hladik C, Mudrak I, Ogris E, Speciale S, White CL, 3rd. Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer disease pathology. J Neuropathol Exp Neurol 2004; 63:287-301; PMID: 15099019
    • (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    White, C.L.7
  • 49
    • 0041589248 scopus 로고    scopus 로고
    • Alpha-Synuclein is degraded by both autophagy and the proteasome
    • PMID:12719433
    • Webb JL, Ravikumar B, Atkins J, Skepper JN, Rubinsztein DC. Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 2003; 278:25009-13; PMID:12719433; http://dx.doi.org/10.1074/jbc.M300227200
    • (2003) J Biol Chem , vol.278 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3    Skepper, J.N.4    Rubinsztein, D.C.5
  • 50
    • 68449089023 scopus 로고    scopus 로고
    • Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric a-synuclein
    • PMID:19628769
    • Yu WH, Dorado B, Figueroa HY, Wang L, Planel E, Cookson MR, Clark LN, Duff KE. Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric a-synuclein. Am J Pathol 2009; 175:736-47; PMID:19628769; http://dx.doi.org/10.2353/ajpath.2009.080928
    • (2009) Am J Pathol , vol.175 , pp. 736-747
    • Yu, W.H.1    Dorado, B.2    Figueroa, H.Y.3    Wang, L.4    Planel, E.5    Cookson, M.R.6    Clark, L.N.7    Duff, K.E.8
  • 51
    • 84874487118 scopus 로고    scopus 로고
    • Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies
    • PMID:23297226
    • Sardi SP, Clarke J, Viel C, Chan M, Tamsett TJ, Treleaven CM, Bu J, Sweet L, Passini MA, Dodge JC, et al. Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies. Proc Natl Acad Sci U S A 2013; 110:3537-42; PMID:23297226; http://dx.doi.org/10.1073/pnas.1220464110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3537-3542
    • Sardi, S.P.1    Clarke, J.2    Viel, C.3    Chan, M.4    Tamsett, T.J.5    Treleaven, C.M.6    Bu, J.7    Sweet, L.8    Passini, M.A.9    Dodge, J.C.10
  • 52
    • 84871720426 scopus 로고    scopus 로고
    • Membranebound a-synuclein interacts with glucocerebrosidase and inhibits enzyme activity
    • PMID:23266198
    • Yap TL, Velayati A, Sidransky E, Lee JC. Membranebound a-synuclein interacts with glucocerebrosidase and inhibits enzyme activity. Mol Genet Metab 2013; 108:56-64; PMID:23266198; http://dx.doi.org/10.1016/j.ymgme.2012.11.010
    • (2013) Mol Genet Metab , vol.108 , pp. 56-64
    • Yap, T.L.1    Velayati, A.2    Sidransky, E.3    Lee, J.C.4
  • 53
    • 0034663039 scopus 로고    scopus 로고
    • The A53T a-synuclein mutation increases iron-dependent aggregation and toxicity
    • PMID:10934254
    • Ostrerova-Golts N, Petrucelli L, Hardy J, Lee JM, Farer M, Wolozin B. The A53T a-synuclein mutation increases iron-dependent aggregation and toxicity. J Neurosci 2000; 20:6048-54; PMID:10934254
    • (2000) J Neurosci , vol.20 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 54
    • 79953191736 scopus 로고    scopus 로고
    • A-Synuclein overexpression impairs mitochondrial function by associating with adenylate translocator
    • PMID:21310263
    • Zhu Y, Duan C, Lu L, Gao H, Zhao C, Yu S, Ueda K, Chan P, Yang H. a-Synuclein overexpression impairs mitochondrial function by associating with adenylate translocator. Int J Biochem Cell Biol 2011; 43:732-41; PMID:21310263; http://dx.doi.org/10.1016/j.biocel.2011.01.014
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 732-741
    • Zhu, Y.1    Duan, C.2    Lu, L.3    Gao, H.4    Zhao, C.5    Yu, S.6    Ueda, K.7    Chan, P.8    Yang, H.9
  • 55
    • 84880184556 scopus 로고    scopus 로고
    • Alpha-synuclein overexpression increases phospho-protein phosphatase 2A levels via formation of calmodulin/Src complex
    • PMID:23796501
    • Yang W, Wang X, Duan C, Lu L, Yang H. Alpha-synuclein overexpression increases phospho-protein phosphatase 2A levels via formation of calmodulin/Src complex. Neurochem Int 2013; 63:180-94; PMID:23796501; http://dx.doi.org/10.1016/j.neuint. 2013.06.010
    • (2013) Neurochem Int , vol.63 , pp. 180-194
    • Yang, W.1    Wang, X.2    Duan, C.3    Lu, L.4    Yang, H.5
  • 56
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • PMID:13428781
    • Folch J, Lees M, Sloane Stanley GH. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem 1957; 226:497-509; PMID:13428781
    • (1957) J Biol Chem , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.