{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,24]],"date-time":"2025-09-24T10:32:44Z","timestamp":1758709964968},"reference-count":50,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,10,1]]},"abstract":"<jats:p>PD (Parkinson's disease) is a neurodegenerative disorder, caused by a selective loss of dopaminergic neurons in the substantia nigra, which affects an increasing number of the elderly population worldwide. One of the major hallmarks of PD is the occurrence of intracellular protein deposits in the dying neurons, termed Lewy bodies, which contain different proteins, including aggregated \u03b1-synuclein and its interacting protein synphilin-1. During the last decade, a number of groups developed yeast models that reproduced important features of PD and allowed the deciphering of pathways underlying the cytotoxicity triggered by \u03b1-synuclein. Here, we review the recent contributions obtained with yeast models designed to study the presumed pathobiology of synphilin-1. These models pointed towards a crucial role of the sirtuin Sir2 and the chaperonin complex TRiC (TCP-1 ring complex)\/CCT (chaperonin containing TCP-1) in handling misfolded and aggregated proteins.<\/jats:p>","DOI":"10.1042\/bst0391476","type":"journal-article","created":{"date-parts":[[2012,5,3]],"date-time":"2012-05-03T12:32:44Z","timestamp":1336048364000},"page":"1476-1481","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Aggresome formation and segregation of inclusions influence toxicity of \u03b1-synuclein and synphilin-1 in yeast"],"prefix":"10.1042","volume":"39","author":[{"given":"Erwin","family":"Swinnen","sequence":"first","affiliation":[{"name":"Functional Biology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 31, 3001 Heverlee, Belgium"}]},{"given":"Sabrina","family":"B\u00fcttner","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biosciences, University of Graz, Graz, Austria"}]},{"given":"Tiago\u00a0F.","family":"Outeiro","sequence":"additional","affiliation":[{"name":"Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Av. Prof. Egas Moniz, Lisboa, Portugal"},{"name":"Instituto de Fisiologia, Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal"},{"name":"Department of Neurodegeneration and Restaurative Research, Center for Molecular Physiology of the Brain, University Medizin Gottingen, Gottingen, Germany"}]},{"given":"Marie-Christine","family":"Galas","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Lille 2, Alzheimer and Tauopathies, rue Michel Polonovski, Lille, France"},{"name":"Inserm UMR 837, Alzheimer and Tauopathies, rue Michel Polonovski, Lille, France"},{"name":"Universit\u00e9 Lille Nord de France, JP Aubert Research Centre, IMPRT, Lille, France"},{"name":"UDSL, Facult\u00e9 de M\u00e9decine-Pole Recherche, Lille, France"},{"name":"CHU-Lille, Lille, France"}]},{"given":"Frank","family":"Madeo","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biosciences, University of Graz, Graz, Austria"}]},{"given":"Joris","family":"Winderickx","sequence":"additional","affiliation":[{"name":"Functional Biology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 31, 3001 Heverlee, Belgium"}]},{"given":"Vanessa","family":"Franssens","sequence":"additional","affiliation":[{"name":"Functional Biology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 31, 3001 Heverlee, Belgium"}]}],"member":"288","published-online":{"date-parts":[[2011,9,21]]},"reference":[{"key":"2021111900465057900_B1","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1080\/02656730500041871","article-title":"Role of molecular chaperones in neurodegenerative disorders","volume":"21","author":"Meriin","year":"2005","journal-title":"Int. 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