메뉴 건너뛰기




Volumn 12, Issue 3, 2016, Pages

Glucocerebrosidase Deficiency in Drosophila Results in α-Synuclein-Independent Protein Aggregation and Neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; GLUCOSIDASE; GLUCOSYLCERAMIDASE;

EID: 84962477435     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1005944     Document Type: Article
Times cited : (68)

References (68)
  • 1
    • 84875312816 scopus 로고    scopus 로고
    • Gaucher disease: a comprehensive review
    • 23510062, .;():–
    • Rosenbloom BE, Weinreb NJ, Gaucher disease: a comprehensive review. Critical reviews in oncogenesis. 2013;18(3):163–75. 23510062.
    • (2013) Critical reviews in oncogenesis , vol.18 , Issue.3 , pp. 163-175
    • Rosenbloom, B.E.1    Weinreb, N.J.2
  • 2
    • 84875929431 scopus 로고    scopus 로고
    • Gaucher disease: insights from a rare Mendelian disorder
    • 23114583, .;():–.; PubMed Central PMCID: PMC4141347
    • Sidransky E, Gaucher disease: insights from a rare Mendelian disorder. Discovery medicine. 2012;14(77):273–81. 23114583; PubMed Central PMCID: PMC4141347.
    • (2012) Discovery medicine , vol.14 , Issue.77 , pp. 273-281
    • Sidransky, E.1
  • 3
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • 23079555, .;():–. Epub 2012/10/20
    • Sidransky E, Lopez G, The link between the GBA gene and parkinsonism. Lancet neurology. 2012;11(11):986–98. Epub 2012/10/20. doi: 10.1016/S1474-4422(12)70190-423079555.
    • (2012) Lancet neurology , vol.11 , Issue.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 4
    • 84887574376 scopus 로고    scopus 로고
    • Glucocerebrosidase mutations and the pathogenesis of Parkinson disease
    • 24219755, .;():–. Epub 2013/11/14
    • Beavan MS, Schapira AH, Glucocerebrosidase mutations and the pathogenesis of Parkinson disease. Annals of medicine. 2013;45(8):511–21. Epub 2013/11/14. doi: 10.3109/07853890.2013.84900324219755.
    • (2013) Annals of medicine , vol.45 , Issue.8 , pp. 511-521
    • Beavan, M.S.1    Schapira, A.H.2
  • 5
    • 0032996131 scopus 로고    scopus 로고
    • Parkinson's syndrome preceding clinical manifestation of Gaucher's disease
    • 10398575, .;():–. Epub 1999/07/09
    • Machaczka M, Rucinska M, Skotnicki AB, Jurczak W, Parkinson's syndrome preceding clinical manifestation of Gaucher's disease. Am J Hematol. 1999;61(3):216–7. Epub 1999/07/09. 10398575.
    • (1999) Am J Hematol , vol.61 , Issue.3 , pp. 216-217
    • Machaczka, M.1    Rucinska, M.2    Skotnicki, A.B.3    Jurczak, W.4
  • 6
    • 0034848419 scopus 로고    scopus 로고
    • Gaucher disease and parkinsonism: a phenotypic and genotypic characterization
    • 11509013, ..;():–. Epub 2001/08/18
    • Tayebi N, Callahan M, Madike V, Stubblefield BK, Orvisky E, Krasnewich D, et al. Gaucher disease and parkinsonism: a phenotypic and genotypic characterization. Mol Genet Metab. 2001;73(4):313–21. Epub 2001/08/18. doi: 10.1006/mgme.2001.320111509013.
    • (2001) Mol Genet Metab , vol.73 , Issue.4 , pp. 313-321
    • Tayebi, N.1    Callahan, M.2    Madike, V.3    Stubblefield, B.K.4    Orvisky, E.5    Krasnewich, D.6
  • 7
    • 33748304674 scopus 로고    scopus 로고
    • Glucocerebrosidase mutations are an important risk factor for Lewy body disorders
    • 16790605, ..;():–
    • Goker-Alpan O, Giasson BI, Eblan MJ, Nguyen J, Hurtig HI, Lee VM, et al. Glucocerebrosidase mutations are an important risk factor for Lewy body disorders. Neurology. 2006;67(5):908–10. doi: 10.1212/01.wnl.0000230215.41296.1816790605.
    • (2006) Neurology , vol.67 , Issue.5 , pp. 908-910
    • Goker-Alpan, O.1    Giasson, B.I.2    Eblan, M.J.3    Nguyen, J.4    Hurtig, H.I.5    Lee, V.M.6
  • 8
    • 40849120549 scopus 로고    scopus 로고
    • Glucocerebrosidase gene mutations: a risk factor for Lewy body disorders
    • 18332251, ..;():–.; PubMed Central PMCID: PMC2826203
    • Mata IF, Samii A, Schneer SH, Roberts JW, Griffith A, Leis BC, et al. Glucocerebrosidase gene mutations: a risk factor for Lewy body disorders. Archives of neurology. 2008;65(3):379–82. doi: 10.1001/archneurol.2007.6818332251; PubMed Central PMCID: PMC2826203.
    • (2008) Archives of neurology , vol.65 , Issue.3 , pp. 379-382
    • Mata, I.F.1    Samii, A.2    Schneer, S.H.3    Roberts, J.W.4    Griffith, A.5    Leis, B.C.6
  • 9
    • 70350319531 scopus 로고    scopus 로고
    • Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease
    • 19846850, ..;():–. Epub 2009/10/23.; PubMed Central PMCID: PMC2856322
    • Sidransky E, Nalls MA, Aasly JO, Aharon-Peretz J, Annesi G, Barbosa ER, et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease. The New England journal of medicine. 2009;361(17):1651–61. Epub 2009/10/23. doi: 10.1056/NEJMoa090128119846850; PubMed Central PMCID: PMC2856322.
    • (2009) The New England journal of medicine , vol.361 , Issue.17 , pp. 1651-1661
    • Sidransky, E.1    Nalls, M.A.2    Aasly, J.O.3    Aharon-Peretz, J.4    Annesi, G.5    Barbosa, E.R.6
  • 10
    • 84922216790 scopus 로고    scopus 로고
    • Gaucher-related synucleinopathies: The examination of sporadic neurodegeneration from a rare (disease) angle
    • 25573151
    • Sardi SP, Cheng SH, Shihabuddin LS, Gaucher-related synucleinopathies: The examination of sporadic neurodegeneration from a rare (disease) angle. Progress in neurobiology. 2015. doi: 10.1016/j.pneurobio.2014.12.00125573151.
    • (2015) Progress in neurobiology
    • Sardi, S.P.1    Cheng, S.H.2    Shihabuddin, L.S.3
  • 11
    • 84899818136 scopus 로고    scopus 로고
    • Glucocerebrosidase is shaking up the synucleinopathies
    • 24531622, .;():–.; PubMed Central PMCID: PMC3999712
    • Siebert M, Sidransky E, Westbroek W, Glucocerebrosidase is shaking up the synucleinopathies. Brain: a journal of neurology. 2014;137(Pt 5):1304–22. doi: 10.1093/brain/awu00224531622; PubMed Central PMCID: PMC3999712.
    • (2014) Brain: a journal of neurology , vol.137 , pp. 1304-1322
    • Siebert, M.1    Sidransky, E.2    Westbroek, W.3
  • 12
    • 0242300619 scopus 로고    scopus 로고
    • alpha-Synuclein locus triplication causes Parkinson's disease
    • 14593171, ..;():
    • Singleton AB, Farrer M, Johnson J, Singleton A, Hague S, Kachergus J, et al. alpha-Synuclein locus triplication causes Parkinson's disease. Science. 2003;302(5646):841. doi: 10.1126/science.109027814593171.
    • (2003) Science , vol.302 , Issue.5646 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3    Singleton, A.4    Hague, S.5    Kachergus, J.6
  • 13
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • 15451224, ..;():–
    • Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, Lincoln S, et al. Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet. 2004;364(9440):1167–9. doi: 10.1016/S0140-6736(04)17103-115451224.
    • (2004) Lancet , vol.364 , Issue.9440 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3    Mouroux, V.4    Douay, X.5    Lincoln, S.6
  • 14
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies
    • 21700325, ..;():–.; PubMed Central PMCID: PMC3132082
    • Mazzulli JR, Xu YH, Sun Y, Knight AL, McLean PJ, Caldwell GA, et al. Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell. 2011;146(1):37–52. doi: 10.1016/j.cell.2011.06.00121700325; PubMed Central PMCID: PMC3132082.
    • (2011) Cell , vol.146 , Issue.1 , 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
  • 16
    • 84983539697 scopus 로고    scopus 로고
    • Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant alpha-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson's disease
    • 26362253, ..;():–
    • Suzuki M, Fujikake N, Takeuchi T, Kohyama-Koganeya A, Nakajima K, Hirabayashi Y, et al. Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant alpha-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson's disease. Human molecular genetics. 2015;24(23):6675–86. doi: 10.1093/hmg/ddv37226362253.
    • (2015) Human molecular genetics , vol.24 , Issue.23 , pp. 6675-6686
    • Suzuki, M.1    Fujikake, N.2    Takeuchi, T.3    Kohyama-Koganeya, A.4    Nakajima, K.5    Hirabayashi, Y.6
  • 17
    • 78650331647 scopus 로고    scopus 로고
    • Identification of functional elements and regulatory circuits by Drosophila modENCODE
    • 21177974, ..;():–.; PubMed Central PMCID: PMC3192495
    • mod EC, Roy S, Ernst J, Kharchenko PV, Kheradpour P, Negre N, et al. Identification of functional elements and regulatory circuits by Drosophila modENCODE. Science. 2010;330(6012):1787–97. doi: 10.1126/science.119837421177974; PubMed Central PMCID: PMC3192495.
    • (2010) Science , vol.330 , Issue.6012 , pp. 1787-1797
    • mod, E.C.1    Roy, S.2    Ernst, J.3    Kharchenko, P.V.4    Kheradpour, P.5    Negre, N.6
  • 18
    • 34249804498 scopus 로고    scopus 로고
    • Using FlyAtlas to identify better Drosophila melanogaster models of human disease
    • 17534367, .;():–
    • Chintapalli VR, Wang J, Dow JA, Using FlyAtlas to identify better Drosophila melanogaster models of human disease. Nature genetics. 2007;39(6):715–20. doi: 10.1038/ng204917534367.
    • (2007) Nature genetics , vol.39 , Issue.6 , pp. 715-720
    • Chintapalli, V.R.1    Wang, J.2    Dow, J.A.3
  • 19
    • 33746384132 scopus 로고    scopus 로고
    • Metabolic disruption in Drosophila bang-sensitive seizure mutants
    • 16648587, .;():–.; PubMed Central PMCID: PMC1526683
    • Fergestad T, Bostwick B, Ganetzky B, Metabolic disruption in Drosophila bang-sensitive seizure mutants. Genetics. 2006;173(3):1357–64. doi: 10.1534/genetics.106.05746316648587; PubMed Central PMCID: PMC1526683.
    • (2006) Genetics , vol.173 , Issue.3 , pp. 1357-1364
    • Fergestad, T.1    Bostwick, B.2    Ganetzky, B.3
  • 20
    • 0020324529 scopus 로고
    • Indirect Suppression Involving Behavioral Mutants with Altered Nerve Excitability in DROSOPHILA MELANOGASTER
    • 17246073, .;():–.; PubMed Central PMCID: PMC1201835
    • Ganetzky B, Wu CF, Indirect Suppression Involving Behavioral Mutants with Altered Nerve Excitability in DROSOPHILA MELANOGASTER. Genetics. 1982;100(4):597–614. 17246073; PubMed Central PMCID: PMC1201835.
    • (1982) Genetics , vol.100 , Issue.4 , pp. 597-614
    • Ganetzky, B.1    Wu, C.F.2
  • 21
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles
    • 11408621, ..;():–. Epub 2001/06/16
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, Hutton M, et al. Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science. 2001;293(5530):711–4. Epub 2001/06/16. doi: 10.1126/science.106238211408621.
    • (2001) Science , vol.293 , Issue.5530 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5    Hutton, M.6
  • 22
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • 15780472, ..;():–. Epub 2005/03/23
    • Crowther DC, Kinghorn KJ, Miranda E, Page R, Curry JA, Duthie FA, et al. Intraneuronal Abeta, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease. Neuroscience. 2005;132(1):123–35. Epub 2005/03/23. doi: 10.1016/j.neuroscience.2004.12.02515780472.
    • (2005) Neuroscience , vol.132 , Issue.1 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3    Page, R.4    Curry, J.A.5    Duthie, F.A.6
  • 23
    • 84887011964 scopus 로고    scopus 로고
    • RNA binding mediates neurotoxicity in the transgenic Drosophila model of TDP-43 proteinopathy
    • 23804749, ..;():–. Epub 2013/06/28
    • Ihara R, Matsukawa K, Nagata Y, Kunugi H, Tsuji S, Chihara T, et al. RNA binding mediates neurotoxicity in the transgenic Drosophila model of TDP-43 proteinopathy. Human molecular genetics. 2013;22(22):4474–84. Epub 2013/06/28. doi: 10.1093/hmg/ddt29623804749.
    • (2013) Human molecular genetics , vol.22 , Issue.22 , pp. 4474-4484
    • Ihara, R.1    Matsukawa, K.2    Nagata, Y.3    Kunugi, H.4    Tsuji, S.5    Chihara, T.6
  • 24
  • 26
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • 18059160, .;():–
    • Simonsen A, Cumming RC, Brech A, Isakson P, Schubert DR, Finley KD, Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy. 2008;4(2):176–84. 18059160.
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 176-184
    • Simonsen, A.1    Cumming, R.C.2    Brech, A.3    Isakson, P.4    Schubert, D.R.5    Finley, K.D.6
  • 27
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging
    • 21111239, .;():–.; PubMed Central PMCID: PMC3066043
    • Demontis F, Perrimon N, FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell. 2010;143(5):813–25. doi: 10.1016/j.cell.2010.10.00721111239; PubMed Central PMCID: PMC3066043.
    • (2010) Cell , vol.143 , Issue.5 , pp. 813-825
    • Demontis, F.1    Perrimon, N.2
  • 28
    • 36849021043 scopus 로고    scopus 로고
    • Atg7-dependent autophagy promotes neuronal health, stress tolerance, and longevity but is dispensable for metamorphosis in Drosophila
    • 18056421, .;():–.; PubMed Central PMCID: PMCPMC2081972
    • Juhasz G, Erdi B, Sass M, Neufeld TP, Atg7-dependent autophagy promotes neuronal health, stress tolerance, and longevity but is dispensable for metamorphosis in Drosophila. Genes Dev. 2007;21(23):3061–6. doi: 10.1101/gad.160070718056421; PubMed Central PMCID: PMCPMC2081972.
    • (2007) Genes Dev , vol.21 , Issue.23 , pp. 3061-3066
    • Juhasz, G.1    Erdi, B.2    Sass, M.3    Neufeld, T.P.4
  • 29
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • 17580304, ..;():–
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. The Journal of biological chemistry. 2007;282(33):24131–45. doi: 10.1074/jbc.M70282420017580304.
    • (2007) The Journal of biological chemistry , vol.282 , Issue.33 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6
  • 30
    • 84923925217 scopus 로고    scopus 로고
    • Monitoring autophagic flux using Ref(2)P, the Drosophila p62 ortholog
    • 25183816, .;():–
    • DeVorkin L, Gorski SM, Monitoring autophagic flux using Ref(2)P, the Drosophila p62 ortholog. Cold Spring Harb Protoc. 2014;2014(9):959–66. doi: 10.1101/pdb.prot08033325183816.
    • (2014) Cold Spring Harb Protoc , vol.2014 , Issue.9 , pp. 959-966
    • DeVorkin, L.1    Gorski, S.M.2
  • 31
    • 84874487118 scopus 로고    scopus 로고
    • Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies
    • 23297226, ..;():–.; PubMed Central PMCID: PMC3587272
    • Sardi SP, Clarke J, Viel C, Chan M, Tamsett TJ, Treleaven CM, et al. Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies. Proceedings of the National Academy of Sciences of the United States of America. 2013;110(9):3537–42. doi: 10.1073/pnas.122046411023297226; PubMed Central PMCID: PMC3587272.
    • (2013) Proceedings of the National Academy of Sciences of the United States of America , vol.110 , Issue.9 , pp. 3537-3542
    • Sardi, S.P.1    Clarke, J.2    Viel, C.3    Chan, M.4    Tamsett, T.J.5    Treleaven, C.M.6
  • 33
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • 15333840, .;():–
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D, Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science. 2004;305(5688):1292–5. doi: 10.1126/science.110173815333840.
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 34
    • 84894528843 scopus 로고    scopus 로고
    • Reduced glucocerebrosidase is associated with increased alpha-synuclein in sporadic Parkinson's disease
    • 24477431, ..;():–.; PubMed Central PMCID: PMC3927701
    • Murphy KE, Gysbers AM, Abbott SK, Tayebi N, Kim WS, Sidransky E, et al. Reduced glucocerebrosidase is associated with increased alpha-synuclein in sporadic Parkinson's disease. Brain: a journal of neurology. 2014;137(Pt 3):834–48. doi: 10.1093/brain/awt36724477431; PubMed Central PMCID: PMC3927701.
    • (2014) Brain: a journal of neurology , 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
  • 35
    • 84965185844 scopus 로고    scopus 로고
    • Loss of glucocerebrosidase 1 activity causes lysosomal dysfunction and alpha-synuclein aggregation
    • 25813221, ..;:
    • Bae EJ, Yang NY, Lee C, Lee HJ, Kim S, Sardi SP, et al. Loss of glucocerebrosidase 1 activity causes lysosomal dysfunction and alpha-synuclein aggregation. Experimental & molecular medicine. 2015;47:e153. doi: 10.1038/emm.2014.12825813221.
    • (2015) Experimental & molecular medicine , vol.47 , pp. e153
    • Bae, E.J.1    Yang, N.Y.2    Lee, C.3    Lee, H.J.4    Kim, S.5    Sardi, S.P.6
  • 36
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • 9809558, .;():–
    • Conway KA, Harper JD, Lansbury PT, Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nature medicine. 1998;4(11):1318–20. doi: 10.1038/33119809558.
    • (1998) Nature medicine , vol.4 , Issue.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 37
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • 23161999, ..;():–.; PubMed Central PMCID: PMC3552321
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ, et al. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science. 2012;338(6109):949–53. doi: 10.1126/science.122715723161999; PubMed Central PMCID: PMC3552321.
    • (2012) Science , vol.338 , Issue.6109 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 38
    • 84907033533 scopus 로고    scopus 로고
    • Addition of exogenous alpha-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous alpha-synuclein to Lewy body and Lewy neurite-like aggregates
    • 25122523, .;():–
    • Volpicelli-Daley LA, Luk KC, Lee VM, Addition of exogenous alpha-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous alpha-synuclein to Lewy body and Lewy neurite-like aggregates. Nature protocols. 2014;9(9):2135–46. doi: 10.1038/nprot.2014.14325122523.
    • (2014) Nature protocols , vol.9 , Issue.9 , pp. 2135-2146
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Lee, V.M.3
  • 39
    • 84876057762 scopus 로고    scopus 로고
    • Prion-like spreading of pathological alpha-synuclein in brain
    • 23466394, ..;():–.; PubMed Central PMCID: PMC3613715
    • Masuda-Suzukake M, Nonaka T, Hosokawa M, Oikawa T, Arai T, Akiyama H, et al. Prion-like spreading of pathological alpha-synuclein in brain. Brain: a journal of neurology. 2013;136(Pt 4):1128–38. doi: 10.1093/brain/awt03723466394; PubMed Central PMCID: PMC3613715.
    • (2013) Brain: a journal of neurology , vol.136 , pp. 1128-1138
    • Masuda-Suzukake, M.1    Nonaka, T.2    Hosokawa, M.3    Oikawa, T.4    Arai, T.5    Akiyama, H.6
  • 40
    • 2542596183 scopus 로고    scopus 로고
    • Parkinson's disease
    • 15172778, .;():–
    • Samii A, Nutt JG, Ransom BR, Parkinson's disease. Lancet. 2004;363(9423):1783–93. doi: 10.1016/S0140-6736(04)16305-815172778.
    • (2004) Lancet , vol.363 , Issue.9423 , pp. 1783-1793
    • Samii, A.1    Nutt, J.G.2    Ransom, B.R.3
  • 41
    • 34547683268 scopus 로고    scopus 로고
    • Non-motor dysfunction in Parkinson's disease
    • 17349813, .;():–
    • Ziemssen T, Reichmann H, Non-motor dysfunction in Parkinson's disease. Parkinsonism & related disorders. 2007;13(6):323–32. doi: 10.1016/j.parkreldis.2006.12.01417349813.
    • (2007) Parkinsonism & related disorders , vol.13 , Issue.6 , pp. 323-332
    • Ziemssen, T.1    Reichmann, H.2
  • 42
    • 84969534214 scopus 로고    scopus 로고
    • Glucocerebrosidase 1 deficient Danio rerio mirror key pathological aspects of human Gaucher disease and provide evidence of early microglial activation preceding alpha-synuclein-independent neuronal cell death
    • 26376862, ..;():–.; PubMed Central PMCID: PMCPMC4634372
    • Keatinge M, Bui H, Menke A, Chen YC, Sokol AM, Bai Q, et al. Glucocerebrosidase 1 deficient Danio rerio mirror key pathological aspects of human Gaucher disease and provide evidence of early microglial activation preceding alpha-synuclein-independent neuronal cell death. Human molecular genetics. 2015;24(23):6640–52. doi: 10.1093/hmg/ddv36926376862; PubMed Central PMCID: PMCPMC4634372.
    • (2015) Human molecular genetics , vol.24 , Issue.23 , pp. 6640-6652
    • Keatinge, M.1    Bui, H.2    Menke, A.3    Chen, Y.C.4    Sokol, A.M.5    Bai, Q.6
  • 43
    • 84930318487 scopus 로고    scopus 로고
    • Viable neuronopathic Gaucher disease model in Medaka (Oryzias latipes) displays axonal accumulation of alpha-synuclein
    • 25835295, ..;():.; PubMed Central PMCID: PMC4383526
    • Uemura N, Koike M, Ansai S, Kinoshita M, Ishikawa-Fujiwara T, Matsui H, et al. Viable neuronopathic Gaucher disease model in Medaka (Oryzias latipes) displays axonal accumulation of alpha-synuclein. PLoS genetics. 2015;11(4):e1005065. doi: 10.1371/journal.pgen.100506525835295; PubMed Central PMCID: PMC4383526.
    • (2015) PLoS genetics , vol.11 , Issue.4 , pp. e1005065
    • Uemura, N.1    Koike, M.2    Ansai, S.3    Kinoshita, M.4    Ishikawa-Fujiwara, T.5    Matsui, H.6
  • 44
    • 84901985544 scopus 로고    scopus 로고
    • Intracellular processing of disease-associated alpha-synuclein in the human brain suggests prion-like cell-to-cell spread
    • 24878508, ..;:–
    • Kovacs GG, Breydo L, Green R, Kis V, Puska G, Lorincz P, et al. Intracellular processing of disease-associated alpha-synuclein in the human brain suggests prion-like cell-to-cell spread. Neurobiol Dis. 2014;69:76–92. doi: 10.1016/j.nbd.2014.05.02024878508.
    • (2014) Neurobiol Dis , vol.69 , pp. 76-92
    • Kovacs, G.G.1    Breydo, L.2    Green, R.3    Kis, V.4    Puska, G.5    Lorincz, P.6
  • 45
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • 10746727, .;():–
    • Feany MB, Bender WW, A Drosophila model of Parkinson's disease. Nature. 2000;404(6776):394–8. doi: 10.1038/3500607410746727.
    • (2000) Nature , vol.404 , Issue.6776 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 46
    • 70350319531 scopus 로고    scopus 로고
    • Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease
    • 19846850, ..;():–. Epub 2009/10/23.; PubMed Central PMCID: PMC2856322
    • Sidransky E, Nalls MA, Aasly JO, Aharon-Peretz J, Annesi G, Barbosa ER, et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease. The New England journal of medicine. 2009;361(17):1651–61. Epub 2009/10/23. doi: 10.1056/NEJMoa090128119846850; PubMed Central PMCID: PMC2856322.
    • (2009) The New England journal of medicine , vol.361 , Issue.17 , pp. 1651-1661
    • Sidransky, E.1    Nalls, M.A.2    Aasly, J.O.3    Aharon-Peretz, J.4    Annesi, G.5    Barbosa, E.R.6
  • 47
    • 77954933661 scopus 로고    scopus 로고
    • The role of glucocerebrosidase mutations in Parkinson disease and Lewy body disorders
    • 20425034, .;():–. Epub 2010/04/29
    • Velayati A, Yu WH, Sidransky E, The role of glucocerebrosidase mutations in Parkinson disease and Lewy body disorders. Curr Neurol Neurosci Rep. 2010;10(3):190–8. Epub 2010/04/29. doi: 10.1007/s11910-010-0102-x20425034.
    • (2010) Curr Neurol Neurosci Rep , vol.10 , Issue.3 , pp. 190-198
    • Velayati, A.1    Yu, W.H.2    Sidransky, E.3
  • 48
    • 70349948789 scopus 로고    scopus 로고
    • Differential phenotype in Parkinson's disease patients with severe versus mild GBA mutations
    • 19502295, .;():. Epub 2009/06/09
    • Gan-Or Z, Giladi N, Orr-Urtreger A, Differential phenotype in Parkinson's disease patients with severe versus mild GBA mutations. Brain: a journal of neurology. 2009;132(Pt 10):e125. Epub 2009/06/09. doi: 10.1093/brain/awp16119502295.
    • (2009) Brain: a journal of neurology , vol.132 , pp. e125
    • Gan-Or, Z.1    Giladi, N.2    Orr-Urtreger, A.3
  • 49
    • 77953229340 scopus 로고    scopus 로고
    • The risk of Parkinson's disease in type 1 Gaucher disease
    • 20177787, ..;():–. Epub 2010/02/24.; PubMed Central PMCID: PMC2887303
    • Bultron G, Kacena K, Pearson D, Boxer M, Yang R, Sathe S, et al. The risk of Parkinson's disease in type 1 Gaucher disease. J Inherit Metab Dis. 2010;33(2):167–73. Epub 2010/02/24. doi: 10.1007/s10545-010-9055-020177787; PubMed Central PMCID: PMC2887303.
    • (2010) J Inherit Metab Dis , vol.33 , Issue.2 , pp. 167-173
    • Bultron, G.1    Kacena, K.2    Pearson, D.3    Boxer, M.4    Yang, R.5    Sathe, S.6
  • 51
    • 24044472010 scopus 로고    scopus 로고
    • Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson's disease
    • 16139213, ..;():–
    • Meulener M, Whitworth AJ, Armstrong-Gold CE, Rizzu P, Heutink P, Wes PD, et al. Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson's disease. Curr Biol. 2005;15(17):1572–7. doi: 10.1016/j.cub.2005.07.06416139213.
    • (2005) Curr Biol , vol.15 , Issue.17 , pp. 1572-1577
    • Meulener, M.1    Whitworth, A.J.2    Armstrong-Gold, C.E.3    Rizzu, P.4    Heutink, P.5    Wes, P.D.6
  • 52
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • 16672981, ..;():–
    • Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, Seol JH, et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature. 2006;441(7097):1162–6. doi: 10.1038/nature0477916672981.
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6
  • 53
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • 16672980, ..;():–
    • Park J, Lee SB, Lee S, Kim Y, Song S, Kim S, et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature. 2006;441(7097):1157–61. doi: 10.1038/nature0478816672980.
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6
  • 54
    • 15544380902 scopus 로고    scopus 로고
    • Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
    • 15689351, .;():–
    • Greene JC, Whitworth AJ, Andrews LA, Parker TJ, Pallanck LJ, Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis. Human molecular genetics. 2005;14(6):799–811. doi: 10.1093/hmg/ddi07415689351.
    • (2005) Human molecular genetics , vol.14 , Issue.6 , pp. 799-811
    • Greene, J.C.1    Whitworth, A.J.2    Andrews, L.A.3    Parker, T.J.4    Pallanck, L.J.5
  • 55
    • 33644862373 scopus 로고    scopus 로고
    • Drosophila models pioneer a new approach to drug discovery for Parkinson's disease
    • 16533709, .;():–
    • Whitworth AJ, Wes PD, Pallanck LJ, Drosophila models pioneer a new approach to drug discovery for Parkinson's disease. Drug Discov Today. 2006;11(3–4):119–26. doi: 10.1016/S1359-6446(05)03693-716533709.
    • (2006) Drug Discov Today , vol.11 , Issue.3-4 , pp. 119-126
    • Whitworth, A.J.1    Wes, P.D.2    Pallanck, L.J.3
  • 56
    • 0037518448 scopus 로고    scopus 로고
    • Salvage pathways in glycosphingolipid metabolism
    • 12770781, .;():–
    • Tettamanti G, Bassi R, Viani P, Riboni L, Salvage pathways in glycosphingolipid metabolism. Biochimie. 2003;85(3–4):423–37. 12770781.
    • (2003) Biochimie , vol.85 , Issue.3-4 , pp. 423-437
    • Tettamanti, G.1    Bassi, R.2    Viani, P.3    Riboni, L.4
  • 57
    • 84872284081 scopus 로고    scopus 로고
    • Ceramide function in the brain: when a slight tilt is enough
    • 22729185, .;():–.; PubMed Central PMCID: PMC3535405
    • Mencarelli C, Martinez-Martinez P, Ceramide function in the brain: when a slight tilt is enough. Cellular and molecular life sciences: CMLS. 2013;70(2):181–203. doi: 10.1007/s00018-012-1038-x22729185; PubMed Central PMCID: PMC3535405.
    • (2013) Cellular and molecular life sciences: CMLS , vol.70 , Issue.2 , pp. 181-203
    • Mencarelli, C.1    Martinez-Martinez, P.2
  • 58
    • 78649790713 scopus 로고    scopus 로고
    • The role of the ceramide acyl chain length in neurodegeneration: involvement of ceramide synthases
    • 20502986, .;():–
    • Ben-David O, Futerman AH, The role of the ceramide acyl chain length in neurodegeneration: involvement of ceramide synthases. Neuromolecular medicine. 2010;12(4):341–50. doi: 10.1007/s12017-010-8114-x20502986.
    • (2010) Neuromolecular medicine , vol.12 , Issue.4 , pp. 341-350
    • Ben-David, O.1    Futerman, A.H.2
  • 60
    • 84884827809 scopus 로고    scopus 로고
    • New insights on glucosylated lipids: metabolism and functions
    • 23770033, .;():–
    • Ishibashi Y, Kohyama-Koganeya A, Hirabayashi Y, New insights on glucosylated lipids: metabolism and functions. Biochim Biophys Acta. 2013;1831(9):1475–85. doi: 10.1016/j.bbalip.2013.06.00123770033.
    • (2013) Biochim Biophys Acta , vol.1831 , Issue.9 , pp. 1475-1485
    • Ishibashi, Y.1    Kohyama-Koganeya, A.2    Hirabayashi, Y.3
  • 61
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits alpha-synuclein fibril formation
    • 12621030, .;():–
    • Zhu M, Fink AL, Lipid binding inhibits alpha-synuclein fibril formation. The Journal of biological chemistry. 2003;278(19):16873–7. doi: 10.1074/jbc.M21013620012621030.
    • (2003) The Journal of biological chemistry , vol.278 , Issue.19 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 62
    • 77956994435 scopus 로고    scopus 로고
    • Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases
    • 20807455, .;:.; PubMed Central PMCID: PMC2931503
    • Fantini J, Yahi N, Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases. Expert Rev Mol Med. 2010;12:e27. doi: 10.1017/S146239941000160220807455; PubMed Central PMCID: PMC2931503.
    • (2010) Expert Rev Mol Med , vol.12 , pp. e27
    • Fantini, J.1    Yahi, N.2
  • 63
    • 84936765095 scopus 로고    scopus 로고
    • Lipids in Amyloid-beta Processing, Aggregation, and Toxicity
    • 26149926, .;:–
    • Morgado I, Garvey M, Lipids in Amyloid-beta Processing, Aggregation, and Toxicity. Adv Exp Med Biol. 2015;855:67–94. doi: 10.1007/978-3-319-17344-3_326149926.
    • (2015) Adv Exp Med Biol , vol.855 , pp. 67-94
    • Morgado, I.1    Garvey, M.2
  • 64
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • 6289436, .;():–
    • Rubin GM, Spradling AC, Genetic transformation of Drosophila with transposable element vectors. Science. 1982;218(4570):348–53. 6289436.
    • (1982) Science , vol.218 , Issue.4570 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 65
    • 0037370716 scopus 로고    scopus 로고
    • Targeted gene expression in Drosophila dopaminergic cells using regulatory sequences from tyrosine hydroxylase
    • 12555273, .;():–
    • Friggi-Grelin F, Coulom H, Meller M, Gomez D, Hirsh J, Birman S, Targeted gene expression in Drosophila dopaminergic cells using regulatory sequences from tyrosine hydroxylase. J Neurobiol. 2003;54(4):618–27. doi: 10.1002/neu.1018512555273.
    • (2003) J Neurobiol , vol.54 , Issue.4 , pp. 618-627
    • Friggi-Grelin, F.1    Coulom, H.2    Meller, M.3    Gomez, D.4    Hirsh, J.5    Birman, S.6
  • 66
    • 79952646811 scopus 로고    scopus 로고
    • Robust RT-qPCR data normalization: validation and selection of internal reference genes during post-experimental data analysis
    • 21423626, .;():.; PubMed Central PMCID: PMCPMC3058000
    • Ling D, Salvaterra PM, Robust RT-qPCR data normalization: validation and selection of internal reference genes during post-experimental data analysis. PloS one. 2011;6(3):e17762. doi: 10.1371/journal.pone.001776221423626; PubMed Central PMCID: PMCPMC3058000.
    • (2011) PloS one , vol.6 , Issue.3 , pp. e17762
    • Ling, D.1    Salvaterra, P.M.2
  • 67
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: an open-source platform for biological-image analysis
    • 22743772, ..;():–.; PubMed Central PMCID: PMC3855844
    • Schindelin J, Arganda-Carreras I, Frise E, Kaynig V, Longair M, Pietzsch T, et al. Fiji: an open-source platform for biological-image analysis. Nat Methods. 2012;9(7):676–82. doi: 10.1038/nmeth.201922743772; PubMed Central PMCID: PMC3855844.
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 676-682
    • Schindelin, J.1    Arganda-Carreras, I.2    Frise, E.3    Kaynig, V.4    Longair, M.5    Pietzsch, T.6
  • 68
    • 0023663064 scopus 로고
    • Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate
    • 2822254, ..;():–
    • Ball E, Karlik CC, Beall CJ, Saville DL, Sparrow JC, Bullard B, et al. Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate. Cell. 1987;51(2):221–8. 2822254.
    • (1987) Cell , vol.51 , Issue.2 , pp. 221-228
    • Ball, E.1    Karlik, C.C.2    Beall, C.J.3    Saville, D.L.4    Sparrow, J.C.5    Bullard, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.