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Volumn 44, Issue , 2017, Pages 74-83

Yeast models of Parkinson's disease-associated molecular pathologies

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; BENZIMIDAZOLE DERIVATIVE; BETA SYNUCLEIN; CYCLOPEPTIDE; GAMMA SYNUCLEIN; LEUCINE RICH REPEAT KINASE 2; N ARYL BENZIMIDAZOLE; PARKIN; SYNPHILIN 1; UNCLASSIFIED DRUG;

EID: 85013224841     PISSN: 0959437X     EISSN: 18790380     Source Type: Journal    
DOI: 10.1016/j.gde.2017.01.013     Document Type: Review
Times cited : (49)

References (105)
  • 1
    • 33645728523 scopus 로고    scopus 로고
    • Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications
    • 1 Skovronsky, D.M., Lee, V.M., Trojanowski, J.Q., Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications. Annu Rev Pathol 1 (2006), 151–170.
    • (2006) Annu Rev Pathol , vol.1 , pp. 151-170
    • Skovronsky, D.M.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • 2 Dobson, C.M., Protein folding and misfolding. Nature 426 (2003), 884–890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 84965178012 scopus 로고    scopus 로고
    • Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology
    • 3 Yang, H., Hu, H.Y., Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology. FEBS J 283:20 (2016), 3705–3717.
    • (2016) FEBS J , vol.283 , Issue.20 , pp. 3705-3717
    • Yang, H.1    Hu, H.Y.2
  • 4
    • 84885176987 scopus 로고    scopus 로고
    • The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity
    • 4 Cecchi, C., Stefani, M., The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity. Biophys Chem 182 (2013), 30–43.
    • (2013) Biophys Chem , vol.182 , pp. 30-43
    • Cecchi, C.1    Stefani, M.2
  • 5
    • 77954122221 scopus 로고    scopus 로고
    • Genome-wide association studies: the key to unlocking neurodegeneration?
    • 5 Gandhi, S., Wood, N.W., Genome-wide association studies: the key to unlocking neurodegeneration?. Nat Neurosci 13 (2010), 789–794.
    • (2010) Nat Neurosci , vol.13 , pp. 789-794
    • Gandhi, S.1    Wood, N.W.2
  • 6
    • 84976351592 scopus 로고    scopus 로고
    • Epigenetic regulation in Parkinson's disease
    • 6 Labbe, C., Lorenzo-Betancor, O., Ross, O.A., Epigenetic regulation in Parkinson's disease. Acta Neuropathol 132:4 (2016), 515–530.
    • (2016) Acta Neuropathol , vol.132 , Issue.4 , pp. 515-530
    • Labbe, C.1    Lorenzo-Betancor, O.2    Ross, O.A.3
  • 7
    • 67649185049 scopus 로고    scopus 로고
    • Genetics, environmental factors and the emerging role of epigenetics in neurodegenerative diseases
    • 7 Migliore, L., Coppede, F., Genetics, environmental factors and the emerging role of epigenetics in neurodegenerative diseases. Mutat Res 667 (2009), 82–97.
    • (2009) Mutat Res , vol.667 , pp. 82-97
    • Migliore, L.1    Coppede, F.2
  • 9
    • 84887934289 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease: the yield
    • 9 Spatola, M., Wider, C., Genetics of Parkinson's disease: the yield. Parkinsonism Relat Disord 20:Suppl. 1 (2014), S35–38.
    • (2014) Parkinsonism Relat Disord , vol.20 , pp. S35-38
    • Spatola, M.1    Wider, C.2
  • 10
    • 84887956934 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease—state of the art, 2013
    • 10 Bonifati, V., Genetics of Parkinson's disease—state of the art, 2013. Parkinsonism Relat Disord 20:Suppl. 1 (2014), S23–S28.
    • (2014) Parkinsonism Relat Disord , vol.20 , pp. S23-S28
    • Bonifati, V.1
  • 12
    • 84941944128 scopus 로고
    • Mitochondria, autophagy and age-associated neurodegenerative diseases: new insights into a complex interplay
    • 12 Lionaki, E., Markaki, M., Palikaras, K., Tavernarakis, N., Mitochondria, autophagy and age-associated neurodegenerative diseases: new insights into a complex interplay. Biochim Biophys Acta 2015 (1847), 1412–1423.
    • (1847) Biochim Biophys Acta , vol.2015 , pp. 1412-1423
    • Lionaki, E.1    Markaki, M.2    Palikaras, K.3    Tavernarakis, N.4
  • 14
    • 20444504698 scopus 로고    scopus 로고
    • The genetic epidemiology of neurodegenerative disease
    • 14 Bertram, L., Tanzi, R.E., The genetic epidemiology of neurodegenerative disease. J Clin Investig 115 (2005), 1449–1457.
    • (2005) J Clin Investig , vol.115 , pp. 1449-1457
    • Bertram, L.1    Tanzi, R.E.2
  • 16
    • 85027920043 scopus 로고    scopus 로고
    • Genetics in Parkinson disease: Mendelian versus non-Mendelian inheritance
    • 16 Hernandez, D.G., Reed, X., Singleton, A.B., Genetics in Parkinson disease: Mendelian versus non-Mendelian inheritance. J Neurochem, 2016, 10.1111/jnc.13593.
    • (2016) J Neurochem
    • Hernandez, D.G.1    Reed, X.2    Singleton, A.B.3
  • 17
    • 85027948388 scopus 로고    scopus 로고
    • The genetic background of Parkinson's disease: current progress and future prospects
    • 17 Kalinderi, K., Bostantjopoulou, S., Fidani, L., The genetic background of Parkinson's disease: current progress and future prospects. Acta Neurol Scand, 2016, 10.1111/ane.12563.
    • (2016) Acta Neurol Scand
    • Kalinderi, K.1    Bostantjopoulou, S.2    Fidani, L.3
  • 18
    • 84973915581 scopus 로고    scopus 로고
    • The evolution of genetics: Alzheimer's and Parkinson's diseases
    • 18 Singleton, A., Hardy, J., The evolution of genetics: Alzheimer's and Parkinson's diseases. Neuron 90 (2016), 1154–1163.
    • (2016) Neuron , vol.90 , pp. 1154-1163
    • Singleton, A.1    Hardy, J.2
  • 22
    • 84885461450 scopus 로고    scopus 로고
    • α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy?
    • 22 Kiely, A.P., Asi, Y.T., Kara, E., Limousin, P., Ling, H., Lewis, P., Proukakis, C., Quinn, N., Lees, A.J., Hardy, J., et al. α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy?. Acta Neuropathol 125 (2013), 753–769.
    • (2013) Acta Neuropathol , vol.125 , pp. 753-769
    • Kiely, A.P.1    Asi, Y.T.2    Kara, E.3    Limousin, P.4    Ling, H.5    Lewis, P.6    Proukakis, C.7    Quinn, N.8    Lees, A.J.9    Hardy, J.10
  • 27
  • 29
    • 34548318990 scopus 로고    scopus 로고
    • Physiological and pathological properties of α-synuclein
    • 29 Tofaris, G.K., Spillantini, M.G., Physiological and pathological properties of α-synuclein. Cell Mol Life Sci 64 (2007), 2194–2201.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2194-2201
    • Tofaris, G.K.1    Spillantini, M.G.2
  • 30
    • 80052967403 scopus 로고    scopus 로고
    • Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study (LRRK2 exonic variants and susceptibility to Parkinson's disease)
    • 30 Ross, O.A., Soto-ortolaza, A.I., Heckman, M.G., Jan, O., Abahuni, N., Annesi, G., Bacon, J.A., Bozi, M., Brice, A., Brighina, L., Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case-control study (LRRK2 exonic variants and susceptibility to Parkinson's disease). Lancet Neurol 10 (2011), 898–908.
    • (2011) Lancet Neurol , vol.10 , pp. 898-908
    • Ross, O.A.1    Soto-ortolaza, A.I.2    Heckman, M.G.3    Jan, O.4    Abahuni, N.5    Annesi, G.6    Bacon, J.A.7    Bozi, M.8    Brice, A.9    Brighina, L.10
  • 31
    • 78649389313 scopus 로고    scopus 로고
    • The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease
    • 31 Cookson, M.R., The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease. Nat Rev Neurosci 11 (2010), 791–797.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 791-797
    • Cookson, M.R.1
  • 32
    • 84979706386 scopus 로고    scopus 로고
    • Activation mechanism of LRRK2 and its cellular functions in Parkinson's disease
    • 32 Rosenbusch, K.E., Kortholt, A., Activation mechanism of LRRK2 and its cellular functions in Parkinson's disease. Parkinsons Dis, 2016, 2016, 7351985.
    • (2016) Parkinsons Dis , vol.2016 , pp. 7351985
    • Rosenbusch, K.E.1    Kortholt, A.2
  • 33
    • 84958567797 scopus 로고    scopus 로고
    • Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
    • Using a combination of phosphoproteomics, genetics and pharmacology Rab GTPases were identified as LRRK2 targets. LRRK2 was shown to directly induce phosphorylation of these Rab GTPases. Moreover, pathogenic LRvariants altered the Rab GTPase phosphorylation level, which also affected their interaction with several regulatory proteins.
    • 33•• Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife, 5, 2016 Using a combination of phosphoproteomics, genetics and pharmacology Rab GTPases were identified as LRRK2 targets. LRRK2 was shown to directly induce phosphorylation of these Rab GTPases. Moreover, pathogenic LRvariants altered the Rab GTPase phosphorylation level, which also affected their interaction with several regulatory proteins.
    • (2016) Elife , vol.5
    • Steger, M.1    Tonelli, F.2    Ito, G.3    Davies, P.4    Trost, M.5    Vetter, M.6    Wachter, S.7    Lorentzen, E.8    Duddy, G.9    Wilson, S.10
  • 38
    • 77149155327 scopus 로고    scopus 로고
    • Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1
    • 38 Tabuchi, M., Yanatori, I., Kawai, Y., Kishi, F., Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1. J Cell Sci 123 (2010), 756–766.
    • (2010) J Cell Sci , vol.123 , pp. 756-766
    • Tabuchi, M.1    Yanatori, I.2    Kawai, Y.3    Kishi, F.4
  • 45
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • 45 Narendra, D., Tanaka, A., Suen, D.F., Youle, R.J., Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183 (2008), 795–803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 46
    • 84928758383 scopus 로고    scopus 로고
    • Evidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1
    • 46 van der Merwe, C., Jalali Sefid Dashti, Z., Christoffels, A., Loos, B., Bardien, S., Evidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1. Eur J Neurosci 41 (2015), 1113–1125.
    • (2015) Eur J Neurosci , vol.41 , pp. 1113-1125
    • van der Merwe, C.1    Jalali Sefid Dashti, Z.2    Christoffels, A.3    Loos, B.4    Bardien, S.5
  • 47
    • 84900475985 scopus 로고    scopus 로고
    • Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phase
    • 47 Miller-Fleming, L., Antas, P., Pais, T.F., Smalley, J.L., Giorgini, F., Outeiro, T.F., Yeast DJ-1 superfamily members are required for diauxic-shift reprogramming and cell survival in stationary phase. Proc Natl Acad Sci U S A 111 (2014), 7012–7017.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 7012-7017
    • Miller-Fleming, L.1    Antas, P.2    Pais, T.F.3    Smalley, J.L.4    Giorgini, F.5    Outeiro, T.F.6
  • 48
    • 84949520315 scopus 로고    scopus 로고
    • Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1
    • In their search for novel PINK1-dependent phosphorylation targets, these researchers identified a subfamily of Rab GTPases, that is, Rab8A, 8B and 13, which are phosphorylated by PINK1 activation at the conserved serine 111 residue (Ser111). However, more detailed analysis demonstrated that Rab8A Ser111 is not directly phosphorylated by PINK1. Furthermore, Rab8 phosphorylation at Ser111 disrupts the interaction with its cognate guanine nucleotide exchange factor (GEF), Rabin8, which in turn impairs its activation.
    • 48•• Lai, Y.C., Kondapalli, C., Lehneck, R., Procter, J.B., Dill, B.D., Woodroof, H.I., Gourlay, R., Peggie, M., Macartney, T.J., Corti, O., et al. Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J 34 (2015), 2840–2861 In their search for novel PINK1-dependent phosphorylation targets, these researchers identified a subfamily of Rab GTPases, that is, Rab8A, 8B and 13, which are phosphorylated by PINK1 activation at the conserved serine 111 residue (Ser111). However, more detailed analysis demonstrated that Rab8A Ser111 is not directly phosphorylated by PINK1. Furthermore, Rab8 phosphorylation at Ser111 disrupts the interaction with its cognate guanine nucleotide exchange factor (GEF), Rabin8, which in turn impairs its activation.
    • (2015) EMBO J , vol.34 , pp. 2840-2861
    • Lai, Y.C.1    Kondapalli, C.2    Lehneck, R.3    Procter, J.B.4    Dill, B.D.5    Woodroof, H.I.6    Gourlay, R.7    Peggie, M.8    Macartney, T.J.9    Corti, O.10
  • 50
    • 84929654352 scopus 로고    scopus 로고
    • The role of ATP13A2 in Parkinson's disease: clinical phenotypes and molecular mechanisms
    • 50 Park, J.-S., Blair, N.F., Sue, C.M., The role of ATP13A2 in Parkinson's disease: clinical phenotypes and molecular mechanisms. Mov Disord 30 (2015), 770–779.
    • (2015) Mov Disord , vol.30 , pp. 770-779
    • Park, J.-S.1    Blair, N.F.2    Sue, C.M.3
  • 52
    • 84860487766 scopus 로고    scopus 로고
    • A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-uncoating co-chaperone auxilin, is associated with juvenile parkinsonism
    • 52 Edvardson, S., Cinnamon, Y., Ta-Shma, A., Shaag, A., Yim, Y.I., Zenvirt, S., Jalas, C., Lesage, S., Brice, A., Taraboulos, A., et al. A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-uncoating co-chaperone auxilin, is associated with juvenile parkinsonism. PLoS One, 7, 2012, e36458.
    • (2012) PLoS One , vol.7 , pp. e36458
    • Edvardson, S.1    Cinnamon, Y.2    Ta-Shma, A.3    Shaag, A.4    Yim, Y.I.5    Zenvirt, S.6    Jalas, C.7    Lesage, S.8    Brice, A.9    Taraboulos, A.10
  • 57
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • 57 Sidransky, E., Lopez, G., The link between the GBA gene and parkinsonism. Lancet Neurol 11 (2012), 986–998.
    • (2012) Lancet Neurol , vol.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 59
    • 84859107964 scopus 로고    scopus 로고
    • Cellular models to investigate biochemical pathways in Parkinson's disease
    • 59 Alberio, T., Lopiano, L., Fasano, M., Cellular models to investigate biochemical pathways in Parkinson's disease. FEBS J 279 (2012), 1146–1155.
    • (2012) FEBS J , vol.279 , pp. 1146-1155
    • Alberio, T.1    Lopiano, L.2    Fasano, M.3
  • 60
    • 84973582082 scopus 로고    scopus 로고
    • iPSCs: on the road to reprogramming aging
    • This review focuses on the different applications of induced pluripotent stem cells (iPSCs) for modelling age-related human disorders such as progeriod syndromes and the neurodegenerative diseases Alzheimer's and Parkinson's. Besides an overview of the available human iPSC models for these diseases, the authors also discuss the potential to use iPSCs in regenerative medicine and their use in drug screening for the identification of novel therapeutic targets.
    • 60• Soria-Valles, C., Lopez-Otin, C., iPSCs: on the road to reprogramming aging. Trends Mol Med 22 (2016), 713–724 This review focuses on the different applications of induced pluripotent stem cells (iPSCs) for modelling age-related human disorders such as progeriod syndromes and the neurodegenerative diseases Alzheimer's and Parkinson's. Besides an overview of the available human iPSC models for these diseases, the authors also discuss the potential to use iPSCs in regenerative medicine and their use in drug screening for the identification of novel therapeutic targets.
    • (2016) Trends Mol Med , vol.22 , pp. 713-724
    • Soria-Valles, C.1    Lopez-Otin, C.2
  • 61
    • 77951558389 scopus 로고    scopus 로고
    • C. elegans as a model organism to investigate molecular pathways involved with Parkinson's disease
    • 61 Harrington, A.J., Hamamichi, S., Caldwell, G.A., Caldwell, K.A., C. elegans as a model organism to investigate molecular pathways involved with Parkinson's disease. Dev Dyn 239 (2010), 1282–1295.
    • (2010) Dev Dyn , vol.239 , pp. 1282-1295
    • Harrington, A.J.1    Hamamichi, S.2    Caldwell, G.A.3    Caldwell, K.A.4
  • 62
    • 84908498272 scopus 로고    scopus 로고
    • Genetic screens in Caenorhabditis elegans models for neurodegenerative diseases
    • This review describes humanized C. elegans models for polyglutamine diseases, Parkinson's and Alzheimer's disease. These models recapitulate faithfully some important aspects of these diseases such as protein aggregation and toxicity. Furthermore, genetic screens performed in the nematod models have been very instrumental in dissecting the mechanisms involved in the development of neurodegenerative disorders.
    • 62• Sin, O., Michels, H., Nollen, E.A., Genetic screens in Caenorhabditis elegans models for neurodegenerative diseases. Biochim Biophys Acta 1842 (2014), 1951–1959 This review describes humanized C. elegans models for polyglutamine diseases, Parkinson's and Alzheimer's disease. These models recapitulate faithfully some important aspects of these diseases such as protein aggregation and toxicity. Furthermore, genetic screens performed in the nematod models have been very instrumental in dissecting the mechanisms involved in the development of neurodegenerative disorders.
    • (2014) Biochim Biophys Acta , vol.1842 , pp. 1951-1959
    • Sin, O.1    Michels, H.2    Nollen, E.A.3
  • 63
    • 84947942460 scopus 로고    scopus 로고
    • Using C. elegans to discover therapeutic compounds for ageing-associated neurodegenerative diseases
    • 63 Chen, X., Barclay, J.W., Burgoyne, R.D., Morgan, A., Using C. elegans to discover therapeutic compounds for ageing-associated neurodegenerative diseases. Chem Cent J, 9, 2015, 65.
    • (2015) Chem Cent J , vol.9 , pp. 65
    • Chen, X.1    Barclay, J.W.2    Burgoyne, R.D.3    Morgan, A.4
  • 64
    • 79551648939 scopus 로고    scopus 로고
    • Drosophila models of Parkinson's disease
    • 64 Whitworth, A.J., Drosophila models of Parkinson's disease. Adv Genet 73 (2011), 1–50.
    • (2011) Adv Genet , vol.73 , pp. 1-50
    • Whitworth, A.J.1
  • 66
    • 84884907135 scopus 로고    scopus 로고
    • A guide to neurotoxic animal models of Parkinson's disease
    • 66 Tieu, K., A guide to neurotoxic animal models of Parkinson's disease. Cold Spring Harb Perspect Med, 1, 2011, a009316.
    • (2011) Cold Spring Harb Perspect Med , vol.1 , pp. a009316
    • Tieu, K.1
  • 67
    • 84946570617 scopus 로고    scopus 로고
    • Age-related neurodegenerative disease research needs aging models
    • This opinion article highlights the relevance of using aging experimental models in age-related neurodegenerative disease research.
    • 67• Johnson, I.P., Age-related neurodegenerative disease research needs aging models. Front Aging Neurosci, 7, 2015, 168 This opinion article highlights the relevance of using aging experimental models in age-related neurodegenerative disease research.
    • (2015) Front Aging Neurosci , vol.7 , pp. 168
    • Johnson, I.P.1
  • 68
    • 84960113368 scopus 로고    scopus 로고
    • Commentary: age-related neurodegenerative disease research needs aging models
    • 68 Wallace, L.M., Howlett, S.E., Commentary: age-related neurodegenerative disease research needs aging models. Front Aging Neurosci, 8, 2016, 9.
    • (2016) Front Aging Neurosci , vol.8 , pp. 9
    • Wallace, L.M.1    Howlett, S.E.2
  • 69
    • 84934983329 scopus 로고    scopus 로고
    • alpha-Synuclein strains cause distinct synucleinopathies after local and systemic administration
    • To investigate the different in vivo properties of α-Synuclein (aSyn) assemblies, aSyn oligomers, fibrils and ribbons were injected in rat brain. This revealed that fibrils are the most toxic strain leading to synaptic impairment and cell death. Additionally, it was shown that propagation of aSyn assemblies is strain dependent and aSyn assemblies are able to cross the blood–brain barrier.
    • 69• Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., Baekelandt, V., alpha-Synuclein strains cause distinct synucleinopathies after local and systemic administration. Nature 522 (2015), 340–344 To investigate the different in vivo properties of α-Synuclein (aSyn) assemblies, aSyn oligomers, fibrils and ribbons were injected in rat brain. This revealed that fibrils are the most toxic strain leading to synaptic impairment and cell death. Additionally, it was shown that propagation of aSyn assemblies is strain dependent and aSyn assemblies are able to cross the blood–brain barrier.
    • (2015) Nature , vol.522 , pp. 340-344
    • Peelaerts, W.1    Bousset, L.2    Van der Perren, A.3    Moskalyuk, A.4    Pulizzi, R.5    Giugliano, M.6    Van den Haute, C.7    Melki, R.8    Baekelandt, V.9
  • 70
    • 84984787903 scopus 로고    scopus 로고
    • Widespread transneuronal propagation of alpha-synucleinopathy triggered in olfactory bulb mimics prodromal Parkinson's disease
    • 70 Rey, N.L., Steiner, J.A., Maroof, N., Luk, K.C., Madaj, Z., Trojanowski, J.Q., Lee, V.M., Brundin, P., Widespread transneuronal propagation of alpha-synucleinopathy triggered in olfactory bulb mimics prodromal Parkinson's disease. J Exp Med 213 (2016), 1759–1778.
    • (2016) J Exp Med , vol.213 , pp. 1759-1778
    • Rey, N.L.1    Steiner, J.A.2    Maroof, N.3    Luk, K.C.4    Madaj, Z.5    Trojanowski, J.Q.6    Lee, V.M.7    Brundin, P.8
  • 71
    • 77952741735 scopus 로고    scopus 로고
    • Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?
    • 71 Khurana, V., Lindquist, S., Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?. Nat Rev Neurosci 11 (2010), 436–449.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 436-449
    • Khurana, V.1    Lindquist, S.2
  • 72
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • 72 Outeiro, T.F., Lindquist, S., Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302 (2003), 1772–1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 74
    • 77949438990 scopus 로고    scopus 로고
    • Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models
    • 74 Su, L.J., Auluck, P.K., Outeiro, T.F., Yeger-Lotem, E., Kritzer, J.A., Tardiff, D.F., Strathearn, K.E., Liu, F., Cao, S., Hamamichi, S., et al. Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Dis Model Mech 3 (2010), 194–208.
    • (2010) Dis Model Mech , vol.3 , pp. 194-208
    • Su, L.J.1    Auluck, P.K.2    Outeiro, T.F.3    Yeger-Lotem, E.4    Kritzer, J.A.5    Tardiff, D.F.6    Strathearn, K.E.7    Liu, F.8    Cao, S.9    Hamamichi, S.10
  • 76
    • 84937677511 scopus 로고    scopus 로고
    • alpha-Synuclein shows high affinity interaction with voltage-dependent anion channel, suggesting mechanisms of mitochondrial regulation and toxicity in Parkinson disease
    • 76 Rostovtseva, T.K., Gurnev, P.A., Protchenko, O., Hoogerheide, D.P., Yap, T.L., Philpott, C.C., Lee, J.C., Bezrukov, S.M., alpha-Synuclein shows high affinity interaction with voltage-dependent anion channel, suggesting mechanisms of mitochondrial regulation and toxicity in Parkinson disease. J Biol Chem 290 (2015), 18467–18477.
    • (2015) J Biol Chem , vol.290 , pp. 18467-18477
    • Rostovtseva, T.K.1    Gurnev, P.A.2    Protchenko, O.3    Hoogerheide, D.P.4    Yap, T.L.5    Philpott, C.C.6    Lee, J.C.7    Bezrukov, S.M.8
  • 77
    • 84864979359 scopus 로고    scopus 로고
    • Aggregate clearance of alpha-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome
    • 77 Petroi, D., Popova, B., Taheri-Talesh, N., Irniger, S., Shahpasandzadeh, H., Zweckstetter, M., Outeiro, T.F., Braus, G.H., Aggregate clearance of alpha-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome. J Biol Chem 287 (2012), 27567–27579.
    • (2012) J Biol Chem , vol.287 , pp. 27567-27579
    • Petroi, D.1    Popova, B.2    Taheri-Talesh, N.3    Irniger, S.4    Shahpasandzadeh, H.5    Zweckstetter, M.6    Outeiro, T.F.7    Braus, G.H.8
  • 80
    • 33751372793 scopus 로고    scopus 로고
    • alpha-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease
    • 80 Witt, S.N., Flower, T.R., alpha-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease. FEMS Yeast Res 6 (2006), 1107–1116.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1107-1116
    • Witt, S.N.1    Flower, T.R.2
  • 83
    • 84861144992 scopus 로고    scopus 로고
    • Suppression of alpha-synuclein toxicity and vesicle trafficking defects by phosphorylation at S129 in yeast depends on genetic context
    • 83 Sancenon, V., Lee, S.A., Patrick, C., Griffith, J., Paulino, A., Outeiro, T.F., Reggiori, F., Masliah, E., Muchowski, P.J., Suppression of alpha-synuclein toxicity and vesicle trafficking defects by phosphorylation at S129 in yeast depends on genetic context. Hum Mol Genet 21 (2012), 2432–2449.
    • (2012) Hum Mol Genet , vol.21 , pp. 2432-2449
    • Sancenon, V.1    Lee, S.A.2    Patrick, C.3    Griffith, J.4    Paulino, A.5    Outeiro, T.F.6    Reggiori, F.7    Masliah, E.8    Muchowski, P.J.9
  • 84
    • 84901361843 scopus 로고    scopus 로고
    • Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease
    • Using yeast cells expressing human aSyn it is demontrated that bloking phosphorylation at S129 alteres the degradation fate of aSyn impairing its degradation via autophagy, increasing inclusions formation and toxicity.
    • 84• Tenreiro, S., Reimao-Pinto, M.M., Antas, P., Rino, J., Wawrzycka, D., Macedo, D., Rosado-Ramos, R., Amen, T., Waiss, M., Magalhaes, F., et al. Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease. PLoS Genet, 10, 2014, e1004302 Using yeast cells expressing human aSyn it is demontrated that bloking phosphorylation at S129 alteres the degradation fate of aSyn impairing its degradation via autophagy, increasing inclusions formation and toxicity.
    • (2014) PLoS Genet , vol.10 , pp. e1004302
    • Tenreiro, S.1    Reimao-Pinto, M.M.2    Antas, P.3    Rino, J.4    Wawrzycka, D.5    Macedo, D.6    Rosado-Ramos, R.7    Amen, T.8    Waiss, M.9    Magalhaes, F.10
  • 85
    • 85012081847 scopus 로고    scopus 로고
    • Posttranslational modifications and clearing of alpha-synuclein aggregates in yeast
    • 85 Popova, B., Kleinknecht, A., Braus, G.H., Posttranslational modifications and clearing of alpha-synuclein aggregates in yeast. Biomolecules 5 (2015), 617–634.
    • (2015) Biomolecules , vol.5 , pp. 617-634
    • Popova, B.1    Kleinknecht, A.2    Braus, G.H.3
  • 86
    • 84909592222 scopus 로고    scopus 로고
    • Interplay between sumoylation and phosphorylation for protection against alpha-synuclein inclusions
    • 86 Shahpasandzadeh, H., Popova, B., Kleinknecht, A., Fraser, P.E., Outeiro, T.F., Braus, G.H., Interplay between sumoylation and phosphorylation for protection against alpha-synuclein inclusions. J Biol Chem 289 (2014), 31224–31240.
    • (2014) J Biol Chem , vol.289 , pp. 31224-31240
    • Shahpasandzadeh, H.1    Popova, B.2    Kleinknecht, A.3    Fraser, P.E.4    Outeiro, T.F.5    Braus, G.H.6
  • 87
    • 84960800242 scopus 로고    scopus 로고
    • Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity
    • Expressing human beta-synuclein (bSyn) in yeast, it was observed that bSyn also forms inclusions and is toxic for yeast cells and shares similar toxicity mechanisms with aSyn, including vesicular trafficking impairment and induction of oxidative stress. Moreover, bSyn forms heterodimers with aSyn in yeast and in human cells.
    • 87• Tenreiro, S., Rosado-Ramos, R., Gerhardt, E., Favretto, F., Magalhaes, F., Popova, B., Becker, S., Zweckstetter, M., Braus, G.H., Outeiro, T.F., Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity. Hum Mol Genet 25 (2016), 275–290 Expressing human beta-synuclein (bSyn) in yeast, it was observed that bSyn also forms inclusions and is toxic for yeast cells and shares similar toxicity mechanisms with aSyn, including vesicular trafficking impairment and induction of oxidative stress. Moreover, bSyn forms heterodimers with aSyn in yeast and in human cells.
    • (2016) Hum Mol Genet , vol.25 , pp. 275-290
    • Tenreiro, S.1    Rosado-Ramos, R.2    Gerhardt, E.3    Favretto, F.4    Magalhaes, F.5    Popova, B.6    Becker, S.7    Zweckstetter, M.8    Braus, G.H.9    Outeiro, T.F.10
  • 89
    • 84897466706 scopus 로고    scopus 로고
    • 2 stress depending on mitochondrial function and endocytosis in a yeast model
    • Using a yeast model, authors described LRRK2 confers cellular protection during oxidative stress depending on mitochondrial function and endocytosis, indicating that these can represent intersecting pathways in the LRRK2 function.
    • 2 stress depending on mitochondrial function and endocytosis in a yeast model. Biochim Biophys Acta 1840 (2014), 2025–2031 Using a yeast model, authors described LRRK2 confers cellular protection during oxidative stress depending on mitochondrial function and endocytosis, indicating that these can represent intersecting pathways in the LRRK2 function.
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 2025-2031
    • Pereira, C.1    Miguel Martins, L.2    Saraiva, L.3
  • 90
    • 84926408656 scopus 로고    scopus 로고
    • A yeast model of the Parkinson's disease-associated protein Parkin
    • 90 Pereira, C., Costa, V., Martins, L.M., Saraiva, L., A yeast model of the Parkinson's disease-associated protein Parkin. Exp Cell Res 333 (2015), 73–79.
    • (2015) Exp Cell Res , vol.333 , pp. 73-79
    • Pereira, C.1    Costa, V.2    Martins, L.M.3    Saraiva, L.4
  • 96
    • 0345189365 scopus 로고    scopus 로고
    • Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein
    • 96 Willingham, S., Outeiro, T.F., DeVit, M.J., Lindquist, S.L., Muchowski, P.J., Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 302 (2003), 1769–1772.
    • (2003) Science , vol.302 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 97
  • 99
    • 84858050446 scopus 로고    scopus 로고
    • ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2
    • 99 Xiong, Y., Yuan, C., Chen, R., Dawson, T.M., Dawson, V.L., ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. J Neurosci 32 (2012), 3877–3886.
    • (2012) J Neurosci , vol.32 , pp. 3877-3886
    • Xiong, Y.1    Yuan, C.2    Chen, R.3    Dawson, T.M.4    Dawson, V.L.5
  • 100
    • 78149449581 scopus 로고    scopus 로고
    • Synphilin-1 enhances alpha-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner
    • 100 Buttner, S., Delay, C., Franssens, V., Bammens, T., Ruli, D., Zaunschirm, S., de Oliveira, R.M., Outeiro, T.F., Madeo, F., Buee, L., et al. Synphilin-1 enhances alpha-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner. PLoS One, 5, 2010, e13700.
    • (2010) PLoS One , vol.5 , pp. e13700
    • Buttner, S.1    Delay, C.2    Franssens, V.3    Bammens, T.4    Ruli, D.5    Zaunschirm, S.6    de Oliveira, R.M.7    Outeiro, T.F.8    Madeo, F.9    Buee, L.10
  • 101
    • 84979500315 scopus 로고    scopus 로고
    • A genome-wide imaging-based screening to identify genes involved in synphilin-1 inclusion formation in Saccharomyces cerevisiae
    • Using yeast cells expressing human synphilin-1, authors identified the interaction networks and components involved in the formation of synphilin-1 inclusions. Evidence is given that synphilin-1 inclusion formation has a cytoprotective effect to the cell.
    • 101•• Zhao, L., Yang, Q., Zheng, J., Zhu, X., Hao, X., Song, J., Lebacq, T., Franssens, V., Winderickx, J., Nystrom, T., et al. A genome-wide imaging-based screening to identify genes involved in synphilin-1 inclusion formation in Saccharomyces cerevisiae. Sci Rep, 6, 2016, 30134 Using yeast cells expressing human synphilin-1, authors identified the interaction networks and components involved in the formation of synphilin-1 inclusions. Evidence is given that synphilin-1 inclusion formation has a cytoprotective effect to the cell.
    • (2016) Sci Rep , vol.6 , pp. 30134
    • Zhao, L.1    Yang, Q.2    Zheng, J.3    Zhu, X.4    Hao, X.5    Song, J.6    Lebacq, T.7    Franssens, V.8    Winderickx, J.9    Nystrom, T.10
  • 102
    • 84875724418 scopus 로고    scopus 로고
    • Phenotypic screens for compounds that target the cellular pathologies underlying Parkinson's disease
    • 102 Tardiff, D.F., Lindquist, S., Phenotypic screens for compounds that target the cellular pathologies underlying Parkinson's disease. Drug Discov Today Technol 10 (2013), e121–128.
    • (2013) Drug Discov Today Technol , vol.10 , pp. e121-128
    • Tardiff, D.F.1    Lindquist, S.2


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