pubmed-article:16893904 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0020179 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0684309 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0600688 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C1415504 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C1704263 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
pubmed-article:16893904 | lifeskim:mentions | umls-concept:C0059438 | lld:lifeskim |
pubmed-article:16893904 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:16893904 | pubmed:dateCreated | 2006-9-4 | lld:pubmed |
pubmed-article:16893904 | pubmed:abstractText | Huntington's disease (HD) is a progressive neurodegenerative disorder for which only symptomatic treatments of limited effectiveness are available. Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. Here, we demonstrate that the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) potently inhibits the aggregation of mutant htt exon 1 protein in a dose-dependent manner. Dot-blot assays and atomic force microscopy studies revealed that EGCG modulates misfolding and oligomerization of mutant htt exon 1 protein in vitro, indicating that it interferes with very early events in the aggregation process. Also, EGCG significantly reduced polyQ-mediated htt protein aggregation and cytotoxicity in an yeast model of HD. When EGCG was fed to transgenic HD flies overexpressing a pathogenic htt exon 1 protein, photoreceptor degeneration and motor function improved. These results indicate that modulators of htt exon 1 misfolding and oligomerization like EGCG are likely to reduce polyQ-mediated toxicity in vivo. Our studies may provide the basis for the development of a novel pharmacotherapy for HD and related polyQ disorders. | lld:pubmed |
pubmed-article:16893904 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:language | eng | lld:pubmed |
pubmed-article:16893904 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16893904 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16893904 | pubmed:month | Sep | lld:pubmed |
pubmed-article:16893904 | pubmed:issn | 0964-6906 | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:MuchowskiPaul... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:WankerErich... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:ThompsonLesli... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:MarshJ... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:EngemannSabin... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:LindquistSusa... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:LegleiterJust... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:WackerJennife... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:DuennwaldMart... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:EhrnhoeferDag... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:MarkovicPhoeb... | lld:pubmed |
pubmed-article:16893904 | pubmed:author | pubmed-author:RoarkMargaret... | lld:pubmed |
pubmed-article:16893904 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16893904 | pubmed:day | 15 | lld:pubmed |
pubmed-article:16893904 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:16893904 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16893904 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16893904 | pubmed:pagination | 2743-51 | lld:pubmed |
pubmed-article:16893904 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:16893904 | pubmed:meshHeading | pubmed-meshheading:16893904... | lld:pubmed |
pubmed-article:16893904 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16893904 | pubmed:articleTitle | Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. | lld:pubmed |
pubmed-article:16893904 | pubmed:affiliation | Max Delbrueck Center for Molecular Medicine, Department of Neuroproteomics, Berlin, Germany. | lld:pubmed |
pubmed-article:16893904 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16893904 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:16893904 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16893904 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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