| pubmed-article:10072437 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0024408 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C1366904 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0384782 | lld:lifeskim |
| pubmed-article:10072437 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:10072437 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10072437 | pubmed:dateCreated | 1999-4-29 | lld:pubmed |
| pubmed-article:10072437 | pubmed:abstractText | Spinocerebellar ataxia type 3, also known as Machado-Joseph disease (SCA3/MJD), is one of at least eight inherited neurodegenerative diseases caused by expansion of a polyglutamine tract in the disease protein. Here we present two lines of evidence implicating the ubiquitin-proteasome pathway in SCA3/MJD pathogenesis. First, studies of both human disease tissue and in vitro models showed redistribution of the 26S proteasome complex into polyglutamine aggregates. In neurons from SCA3/MJD brain, the proteasome localized to intranuclear inclusions containing the mutant protein, ataxin-3. In transfected cells, the proteasome redistributed into inclusions formed by three expanded polyglutamine proteins: a pathologic ataxin-3 fragment, full-length mutant ataxin-3 and an unrelated GFP-polyglutamine fusion protein. Inclusion formation by the full-length mutant ataxin-3 required nuclear localization of the protein and occurred within specific subnuclear structures recently implicated in the regulation of cell death, promyelocytic leukemia antigen oncogenic domains. In a second set of experiments, inhibitors of the proteasome caused a repeat length-dependent increase in aggregate formation, implying that the proteasome plays a direct role in suppressing polyglutamine aggregation in disease. These results support a central role for protein misfolding in the pathogenesis of SCA3/MJD and suggest that modulating proteasome activity is a potential approach to altering the progression of this and other polyglutamine diseases. | lld:pubmed |
| pubmed-article:10072437 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10072437 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10072437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10072437 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10072437 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10072437 | pubmed:issn | 0964-6906 | lld:pubmed |
| pubmed-article:10072437 | pubmed:author | pubmed-author:ChaiYY | lld:pubmed |
| pubmed-article:10072437 | pubmed:author | pubmed-author:PerezM KMK | lld:pubmed |
| pubmed-article:10072437 | pubmed:author | pubmed-author:PaulsonH LHL | lld:pubmed |
| pubmed-article:10072437 | pubmed:author | pubmed-author:KoppenhaferS... | lld:pubmed |
| pubmed-article:10072437 | pubmed:author | pubmed-author:ShoesmithS... | lld:pubmed |
| pubmed-article:10072437 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10072437 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:10072437 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10072437 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10072437 | pubmed:pagination | 673-82 | lld:pubmed |
| pubmed-article:10072437 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10072437 | pubmed:meshHeading | pubmed-meshheading:10072437... | lld:pubmed |
| pubmed-article:10072437 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10072437 | pubmed:articleTitle | Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. | lld:pubmed |
| pubmed-article:10072437 | pubmed:affiliation | Department of Neurology, University of Iowa College of Medicine, Iowa City, IA 52242, USA. | lld:pubmed |
| pubmed-article:10072437 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10072437 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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