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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5837
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pubmed:dateCreated |
2007-7-27
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pubmed:abstractText |
The sirtuins are members of the histone deacetylase family of proteins that participate in a variety of cellular functions and play a role in aging. We identified a potent inhibitor of sirtuin 2 (SIRT2) and found that inhibition of SIRT2 rescued alpha-synuclein toxicity and modified inclusion morphology in a cellular model of Parkinson's disease. Genetic inhibition of SIRT2 via small interfering RNA similarly rescued alpha-synuclein toxicity. Furthermore, the inhibitors protected against dopaminergic cell death both in vitro and in a Drosophila model of Parkinson's disease. The results suggest a link between neurodegeneration and aging.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Furans,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolines,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SIRT2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
pubmed-author:AbagyanRubenR,
pubmed-author:AltmannStephen MSM,
pubmed-author:AmoreAllison MAM,
pubmed-author:FeanyMel BMB,
pubmed-author:HymanBradley TBT,
pubmed-author:KazantsevAleksey GAG,
pubmed-author:KontopoulosEireneE,
pubmed-author:KufarevaIrinaI,
pubmed-author:MaxwellMichele MMM,
pubmed-author:McLeanPamela JPJ,
pubmed-author:OuteiroTiago FlemingTF,
pubmed-author:RochetJean-ChristopheJC,
pubmed-author:StrathearnKatherine EKE,
pubmed-author:VolkCatherine BCB,
pubmed-author:YoungAnne BAB
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pubmed:issnType |
Electronic
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pubmed:day |
27
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pubmed:volume |
317
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
516-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17588900-Acetylation,
pubmed-meshheading:17588900-Animals,
pubmed-meshheading:17588900-Animals, Genetically Modified,
pubmed-meshheading:17588900-Cell Death,
pubmed-meshheading:17588900-Cell Line, Tumor,
pubmed-meshheading:17588900-Cells, Cultured,
pubmed-meshheading:17588900-Disease Models, Animal,
pubmed-meshheading:17588900-Dopamine,
pubmed-meshheading:17588900-Dose-Response Relationship, Drug,
pubmed-meshheading:17588900-Drosophila melanogaster,
pubmed-meshheading:17588900-Furans,
pubmed-meshheading:17588900-Humans,
pubmed-meshheading:17588900-Models, Molecular,
pubmed-meshheading:17588900-Neurons,
pubmed-meshheading:17588900-Parkinson Disease,
pubmed-meshheading:17588900-Protein Conformation,
pubmed-meshheading:17588900-Quinolines,
pubmed-meshheading:17588900-RNA, Small Interfering,
pubmed-meshheading:17588900-Rats,
pubmed-meshheading:17588900-Sirtuin 1,
pubmed-meshheading:17588900-Sirtuin 2,
pubmed-meshheading:17588900-Sirtuins,
pubmed-meshheading:17588900-Transfection,
pubmed-meshheading:17588900-Tubulin,
pubmed-meshheading:17588900-alpha-Synuclein
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pubmed:year |
2007
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pubmed:articleTitle |
Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease.
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pubmed:affiliation |
Alzheimer's Research Unit, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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