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Volumn 8, Issue 5, 2012, Pages 754-766

Alpha-synuclein aggregation involves a bafilomycin A1-sensitive autophagy pathway

Author keywords

Alpha synuclein; Dementia with lewy bodies (DLB); Lewy body; Lysosomal degradation; Parkinson disease (PD); Protein aggregation

Indexed keywords

ALPHA SYNUCLEIN; BAFILOMYCIN A1;

EID: 84862598619     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.19371     Document Type: Article
Times cited : (109)

References (51)
  • 2
    • 33646197357 scopus 로고    scopus 로고
    • Clinical and biochemical correlates of insoluble alpha-synuclein in dementia with Lewy bodies
    • PMID:16482476
    • Klucken J, Ingelsson M, Shin Y, Irizarry MC, Hedley-Whyte ET, Frosch MP, et al. Clinical and biochemical correlates of insoluble alpha-synuclein in dementia with Lewy bodies. Acta Neuropathol 2006; 111:101-8; PMID:16482476; http://dx.doi.org/10.1007/s00401-005-0027-7
    • (2006) Acta Neuropathol , vol.111 , pp. 101-108
    • Klucken, J.1    Ingelsson, M.2    Shin, Y.3    Irizarry, M.C.4    Hedley-Whyte, E.T.5    Frosch, M.P.6
  • 3
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • PMID:14593166
    • Dawson TM, Dawson VL. Molecular pathways of neurodegeneration in Parkinson's disease. Science 2003; 302:819-22; PMID:14593166; http://dx.doi.org/10.1126/science.1087753
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 4
    • 65549099222 scopus 로고    scopus 로고
    • All-you-can-eat: Autophagy in neurodegeneration and neuroprotection
    • PMID:19348680
    • Jaeger PA, Wyss-Coray T. All-you-can-eat: autophagy in neurodegeneration and neuroprotection. Mol Neurodegener 2009; 4:16; PMID:19348680; http://dx.doi.org/10.1186/1750-1326-4-16
    • (2009) Mol Neurodegener , vol.4 , pp. 16
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 6
    • 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
  • 7
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • PMID:15333840
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004; 305:1292-5; PMID:15333840; http://dx.doi.org/10.1126/science.1101738
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 8
    • 80054026084 scopus 로고    scopus 로고
    • Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of a-synuclein
    • PMID: 21994367
    • Ebrahimi-Fakhari D, Cantuti-Castelvetri I, Fan Z, Rockenstein E, Masliah E, Hyman BT, et al. Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of a-synuclein. J Neurosci 2011; 31:14508-20; PMID: 21994367; http://dx.doi.org/10.1523/JNEUROSCI. 1560-11.2011
    • (2011) J Neurosci , vol.31 , pp. 14508-14520
    • Ebrahimi-Fakhari, D.1    Cantuti-Castelvetri, I.2    Fan, Z.3    Rockenstein, E.4    Masliah, E.5    Hyman, B.T.6
  • 9
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • PMID:17051204
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006; 443:780-6; PMID:17051204; http://dx.doi.org/10.1038/nature05291
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 10
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • PMID:17404494
    • Dice JF. Chaperone-mediated autophagy. Autophagy 2007; 3:295-9; PMID:17404494
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 11
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole
    • PMID:2161853
    • Dunn WA, Jr. Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. J Cell Biol 1990; 110:1935-45; PMID:2161853; http://dx.doi.org/10.1083/jcb.110.6.1935
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn Jr., W.A.1
  • 12
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • PMID:14985429
    • Lee HJ, Khoshaghideh F, Patel S, Lee SJ. Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci 2004; 24: 1888-96; PMID:14985429; http://dx.doi.org/10.1523/JNEUROSCI.3809-03.2004
    • (2004) J Neurosci , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 13
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • PMID:19436756
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L. Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS One 2009; 4:e5515; PMID:19436756; http://dx.doi.org/10.1371/journal.pone.0005515
    • (2009) PLoS One , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 14
    • 68449089023 scopus 로고    scopus 로고
    • Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein
    • PMID:19628769
    • Yu WH, Dorado B, Figueroa HY, Wang L, Planel E, Cookson MR, et al. Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-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
  • 15
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 reduces alpha-synuclein aggregation and toxicity
    • PMID:15044495
    • Klucken J, Shin Y, Masliah E, Hyman BT, McLean PJ. Hsp70 reduces alpha-synuclein aggregation and toxicity. J Biol Chem 2004; 279:25497-502; PMID:15044495; http://dx.doi.org/10.1074/jbc.M400255200
    • (2004) J Biol Chem , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 16
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • PMID:11823645
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 2002; 295:865-8; PMID:11823645; http://dx.doi.org/10.1126/ science.1067389
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 17
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging
    • PMID:17012257
    • Klucken J, Outeiro TF, Nguyen P, McLean PJ, Hyman BT. Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging. FASEB J 2006; 20:2050-7; PMID:17012257; http://dx.doi.org/10.1096/fj. 05-5422com
    • (2006) FASEB J , vol.20 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 18
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • PMID:10678833
    • Masliah E, Rockenstein E, Veinbergs I, Mallory M, Hashimoto M, Takeda A, et al. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 2000; 287:1265-9; PMID:10678833; http://dx.doi.org/10.1126/science.287.5456.1265
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6
  • 19
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • PMID:19864570
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, et al. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's 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
  • 20
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • PMID: 15845543
    • Shin Y, Klucken J, Patterson C, Hyman BT, McLean PJ. The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J Biol Chem 2005; 280:23727-34; PMID: 15845543; http://dx.doi.org/10.1074/jbc.M503326200
    • (2005) J Biol Chem , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 21
    • 79953167820 scopus 로고    scopus 로고
    • Localization of MAP1-LC3 in vulnerable neurons and Lewy bodies in brains of patients with dementia with Lewy bodies
    • PMID:21412173
    • Higashi S, Moore DJ, Minegishi M, Kasanuki K, Fujishiro H, Kabuta T, et al. Localization of MAP1-LC3 in vulnerable neurons and Lewy bodies in brains of patients with dementia with Lewy bodies. J Neuropathol Exp Neurol 2011; 70:264-80; PMID:21412173; http://dx.doi.org/10.1097/NEN.0b013e318211c86a
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 264-280
    • Higashi, S.1    Moore, D.J.2    Minegishi, M.3    Kasanuki, K.4    Fujishiro, H.5    Kabuta, T.6
  • 22
    • 79960226234 scopus 로고    scopus 로고
    • Alteration of autophagosomal proteins (LC3, GABARAP and GATE-16) in Lewy body disease
    • PMID:21684337
    • Tanji K, Mori F, Kakita A, Takahashi H, Wakabayashi K. Alteration of autophagosomal proteins (LC3, GABARAP and GATE-16) in Lewy body disease. Neurobiol Dis 2011; 43:690-7; PMID:21684337; http://dx.doi.org/10.1016/j.nbd. 2011.05.022
    • (2011) Neurobiol Dis , vol.43 , pp. 690-697
    • Tanji, K.1    Mori, F.2    Kakita, A.3    Takahashi, H.4    Wakabayashi, K.5
  • 23
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • PMID:20174468
    • Crews L, Spencer B, Desplats P, Patrick C, Paulino A, Rockenstein E, et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS One 2010; 5:e9313; PMID:20174468; http://dx.doi.org/10.1371/journal.pone.0009313
    • (2010) PLoS One , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6
  • 24
    • 0035859226 scopus 로고    scopus 로고
    • Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • PMID:11440819
    • McLean PJ, Kawamata H, Hyman BT. Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 2001; 104:901-12; PMID:11440819; http://dx.doi.org/10.1016/S0306-4522(01)00113-0
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3
  • 25
    • 33745859721 scopus 로고    scopus 로고
    • Autophagy, bafilomycin and cell death: The "a-B-cs" of plecomacrolide-induced neuroprotection
    • PMID:16874105
    • Shacka JJ, Klocke BJ, Roth KA. Autophagy, bafilomycin and cell death: the "a-B-cs" of plecomacrolide-induced neuroprotection. Autophagy 2006; 2:228-30; PMID:16874105
    • (2006) Autophagy , vol.2 , pp. 228-230
    • Shacka, J.J.1    Klocke, B.J.2    Roth, K.A.3
  • 27
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • PMID:12923179
    • Tofaris GK, Razzaq A, Ghetti B, Lilley KS, Spillantini MG. Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J Biol Chem 2003; 278:44405-11; PMID:12923179; http://dx.doi.org/10.1074/jbc.M308041200
    • (2003) J Biol Chem , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 28
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • PMID:15355963
    • Shao E, Forgac M. Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J Biol Chem 2004; 279:48663-70; PMID:15355963; http://dx.doi.org/10.1074/jbc.M408278200
    • (2004) J Biol Chem , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 29
    • 77956855813 scopus 로고    scopus 로고
    • Pathogenic lysosomal depletion in Parkinson's disease
    • PMID:20844148
    • Dehay B, Bové J, Rodríguez-Muela N, Perier C, Recasens A, Boya P, et al. Pathogenic lysosomal depletion in Parkinson's disease. J Neurosci 2010; 30:12535-44; PMID:20844148; http://dx.doi.org/10.1523/JNEUROSCI.1920-10. 2010
    • (2010) J Neurosci , vol.30 , pp. 12535-12544
    • Dehay, B.1    Bové, J.2    Rodríguez-Muela, N.3    Perier, C.4    Recasens, A.5    Boya, P.6
  • 30
    • 77951541740 scopus 로고    scopus 로고
    • Lysosomal degradation of alpha-synuclein in vivo
    • PMID:20200163
    • Mak SK, McCormack AL, Manning-Bog AB, Cuervo AM, Di Monte DA. Lysosomal degradation of alpha-synuclein in vivo. J Biol Chem 2010; 285:13621-9; PMID:20200163; http://dx.doi.org/10.1074/jbc.M109.074617
    • (2010) J Biol Chem , vol.285 , pp. 13621-13629
    • Mak, S.K.1    McCormack, A.L.2    Manning-Bog, A.B.3    Cuervo, A.M.4    Di Monte, D.A.5
  • 32
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: Relationship to alpha-synuclein inclusions
    • PMID:19505575
    • Chu Y, Dodiya H, Aebischer P, Olanow CW, Kordower JH. Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol Dis 2009; 35:385-98; PMID:19505575; http://dx.doi.org/10.1016/j.nbd.2009.05.023
    • (2009) Neurobiol Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 33
    • 57349133846 scopus 로고    scopus 로고
    • Identification of quinolines that inhibit melanogenesis by altering tyrosinase family trafficking
    • PMID:18801917
    • Ni-Komatsu L, Tong C, Chen G, Brindzei N, Orlow SJ. Identification of quinolines that inhibit melanogenesis by altering tyrosinase family trafficking. Mol Pharmacol 2008; 74:1576-86; PMID:18801917; http://dx.doi.org/10.1124/mol. 108.050633
    • (2008) Mol Pharmacol , vol.74 , pp. 1576-1586
    • Ni-Komatsu, L.1    Tong, C.2    Chen, G.3    Brindzei, N.4    Orlow, S.J.5
  • 34
    • 21044442669 scopus 로고    scopus 로고
    • Lysosomal pathology associated with alpha-synuclein accumulation in transgenic models using an eGFP fusion protein
    • PMID:15765523
    • Rockenstein E, Schwach G, Ingolic E, Adame A, Crews L, Mante M, et al. Lysosomal pathology associated with alpha-synuclein accumulation in transgenic models using an eGFP fusion protein. J Neurosci Res 2005; 80:247-59; PMID:15765523; http://dx.doi.org/10.1002/jnr.20446
    • (2005) J Neurosci Res , vol.80 , pp. 247-259
    • Rockenstein, E.1    Schwach, G.2    Ingolic, E.3    Adame, A.4    Crews, L.5    Mante, M.6
  • 35
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • PMID:11739566
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, Greene LA. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 2001; 21:9549-60; PMID:11739566
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 37
    • 33751034682 scopus 로고    scopus 로고
    • Aggregate-prone proteins are cleared from the cytosol by autophagy: Therapeutic implications
    • PMID:17118264
    • Williams A, Jahreiss L, Sarkar S, Saiki S, Menzies FM, Ravikumar B, et al. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications. Curr Top Dev Biol 2006; 76:89-101; PMID:17118264; http://dx.doi.org/10.1016/S0070-2153(06)76003-3
    • (2006) Curr Top Dev Biol , vol.76 , pp. 89-101
    • Williams, A.1    Jahreiss, L.2    Sarkar, S.3    Saiki, S.4    Menzies, F.M.5    Ravikumar, B.6
  • 38
    • 0028971173 scopus 로고
    • Vanadate and bafilomycin A1 are potent inhibitors of the ATPase activity of the reconstituted bacterial ATP-binding cassette transporter for maltose (MalFGK2)
    • PMID: 7488152
    • Hunke S, Döse S, Schneider E. Vanadate and bafilomycin A1 are potent inhibitors of the ATPase activity of the reconstituted bacterial ATP-binding cassette transporter for maltose (MalFGK2). Biochem Biophys Res Commun 1995; 216:589-94; PMID: 7488152; http://dx.doi.org/10.1006/bbrc.1995.2663
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 589-594
    • Hunke, S.1    Döse, S.2    Schneider, E.3
  • 39
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • PMID:7772017
    • Sharom FJ, Yu X, Chu JW, Doige CA. Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem J 1995; 308:381-90; PMID:7772017
    • (1995) Biochem J , vol.308 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.3    Doige, C.A.4
  • 40
    • 35648957732 scopus 로고    scopus 로고
    • Bafilomycin A1 is a potassium ionophore that impairs mitochondrial functions
    • PMID:17917797
    • Teplova VV, Tonshin AA, Grigoriev PA, Saris NE, Salkinoja-Salonen MS. Bafilomycin A1 is a potassium ionophore that impairs mitochondrial functions. J Bioenerg Biomembr 2007; 39:321-9; PMID:17917797; http://dx.doi.org/10.1007/ s10863-007-9095-9
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 321-329
    • Teplova, V.V.1    Tonshin, A.A.2    Grigoriev, P.A.3    Saris, N.E.4    Salkinoja-Salonen, M.S.5
  • 41
    • 33645100369 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons
    • PMID:16391239
    • Shacka JJ, Klocke BJ, Shibata M, Uchiyama Y, Datta G, Schmidt RE, et al. Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons. Mol Pharmacol 2006; 69:1125-36; PMID:16391239; http://dx.doi.org/10.1124/mol. 105.018408
    • (2006) Mol Pharmacol , vol.69 , pp. 1125-1136
    • Shacka, J.J.1    Klocke, B.J.2    Shibata, M.3    Uchiyama, Y.4    Datta, G.5    Schmidt, R.E.6
  • 42
    • 23844483152 scopus 로고    scopus 로고
    • The apoptosis/autophagy paradox: Autophagic vacuolization before apoptotic death
    • PMID:15985464
    • González-Polo RA, Boya P, Pauleau AL, Jalil A, Larochette N, Souquère S, et al. The apoptosis/autophagy paradox: autophagic vacuolization before apoptotic death. J Cell Sci 2005; 118:3091-102; PMID:15985464; http://dx.doi.org/10.1242/jcs.02447
    • (2005) J Cell Sci , vol.118 , pp. 3091-3102
    • González-Polo, R.A.1    Boya, P.2    Pauleau, A.L.3    Jalil, A.4    Larochette, N.5    Souquère, S.6
  • 43
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • PMID: 17486044
    • Sarkar S, Perlstein EO, Imarisio S, Pineau S, Cordenier A, Maglathlin RL, et al. Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat Chem Biol 2007; 3:331-8; PMID: 17486044; http://dx.doi.org/10.1038/nchembio883
    • (2007) Nat Chem Biol , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3    Pineau, S.4    Cordenier, A.5    Maglathlin, R.L.6
  • 44
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • PMID:17182613
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 2007; 282:5641-52; PMID:17182613; http://dx.doi.org/10.1074/jbc.M609532200
    • (2007) J Biol Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 45
    • 0006164301 scopus 로고    scopus 로고
    • Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): Report of the consortium on DLB international workshop
    • PMID:8909416
    • McKeith IG, Galasko D, Kosaka K, Perry EK, Dickson DW, Hansen LA, et al. Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology 1996; 47:1113-24; PMID:8909416
    • (1996) Neurology , vol.47 , pp. 1113-1124
    • McKeith, I.G.1    Galasko, D.2    Kosaka, K.3    Perry, E.K.4    Dickson, D.W.5    Hansen, L.A.6
  • 46
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters
    • PMID: 12111846
    • Rockenstein E, Mallory M, Hashimoto M, Song D, Shults CW, Lang I, et al. Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J Neurosci Res 2002; 68:568-78; PMID: 12111846; http://dx.doi.org/10.1002/jnr. 10231
    • (2002) J Neurosci Res , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.W.5    Lang, I.6
  • 47
    • 0034958897 scopus 로고    scopus 로고
    • Role of apolipoprotein e receptors in regulating the differential in vivo neurotrophic effects of apolipoprotein e
    • PMID:11421580
    • Veinbergs I, Van Uden E, Mallory M, Alford M, McGiffert C, DeTeresa R, et al. Role of apolipoprotein E receptors in regulating the differential in vivo neurotrophic effects of apolipoprotein E. Exp Neurol 2001; 170:15-26; PMID:11421580; http://dx.doi.org/10.1006/exnr.2001.7684
    • (2001) Exp Neurol , vol.170 , pp. 15-26
    • Veinbergs, I.1    Van Uden, E.2    Mallory, M.3    Alford, M.4    McGiffert, C.5    DeTeresa, R.6
  • 48
    • 0034996655 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein and synphilin-1: Effect of Parkinson's disease-associated mutations
    • PMID:11331421
    • Kawamata H, McLean PJ, Sharma N, Hyman BT. Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations. J Neurochem 2001; 77:929-34; PMID:11331421; http://dx.doi.org/10.1046/j.1471-4159. 2001.00301.x
    • (2001) J Neurochem , vol.77 , pp. 929-934
    • Kawamata, H.1    McLean, P.J.2    Sharma, N.3    Hyman, B.T.4
  • 49
    • 44349187279 scopus 로고    scopus 로고
    • The importance of particle size and DNA condensation salt for calcium phosphate nanoparticle transfection
    • PMID:18485472
    • Pedraza CE, Bassett DC, McKee MD, Nelea V, Gbureck U, Barralet JE. The importance of particle size and DNA condensation salt for calcium phosphate nanoparticle transfection. Biomaterials 2008; 29:3384-92; PMID:18485472; http://dx.doi.org/10.1016/j.biomaterials.2008.04.043
    • (2008) Biomaterials , vol.29 , pp. 3384-3392
    • Pedraza, C.E.1    Bassett, D.C.2    McKee, M.D.3    Nelea, V.4    Gbureck, U.5    Barralet, J.E.6
  • 50
    • 27744515121 scopus 로고    scopus 로고
    • Dominant mutations of Col4a1 result in basementmembrane defects which lead to anterior segment dysgenesis and glomerulopathy
    • PMID: 16159887
    • Van Agtmael T, Schlötzer-Schrehardt U, McKie L, Brownstein DG, Lee AW, Cross SH, et al. Dominant mutations of Col4a1 result in basementmembrane defects which lead to anterior segment dysgenesis and glomerulopathy. Hum Mol Genet 2005; 14:3161-8; PMID: 16159887; http://dx.doi.org/10.1093/hmg/ddi348
    • (2005) Hum Mol Genet , vol.14 , pp. 3161-3168
    • Van Agtmael, T.1    Schlötzer-Schrehardt, U.2    McKie, L.3    Brownstein, D.G.4    Lee, A.W.5    Cross, S.H.6
  • 51
    • 77954358003 scopus 로고    scopus 로고
    • Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins
    • PMID:20573181
    • Pham E, Crews L, Ubhi K, Hansen L, Adame A, Cartier A, et al. Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins. FEBS J 2010; 277:3051-67; PMID:20573181; http://dx.doi.org/10.1111/j.1742-4658.2010.07719.x
    • (2010) FEBS J , vol.277 , pp. 3051-3067
    • Pham, E.1    Crews, L.2    Ubhi, K.3    Hansen, L.4    Adame, A.5    Cartier, A.6


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