| pubmed-article:20730854 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20730854 | lifeskim:mentions | umls-concept:C0020179 | lld:lifeskim |
| pubmed-article:20730854 | lifeskim:mentions | umls-concept:C0033679 | lld:lifeskim |
| pubmed-article:20730854 | lifeskim:mentions | umls-concept:C0277785 | lld:lifeskim |
| pubmed-article:20730854 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:20730854 | lifeskim:mentions | umls-concept:C0005486 | lld:lifeskim |
| pubmed-article:20730854 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:20730854 | pubmed:dateCreated | 2010-9-7 | lld:pubmed |
| pubmed-article:20730854 | pubmed:abstractText | The article by McConoughey et al in the current issue of EMBO Molecular Medicine examines the contribution of transglutaminase 2 (TG2) to Huntington's disease (HD) pathogenesis. The authors find that TG2 inhibition can ameliorate HD neurodegeneration, and thereby elevate the status of transglutaminases (TGs) to a major therapeutic target-not because of their well-known activity in mutant protein aggregation, but instead based upon their ability to epigenetically modulate transcription and energy production. While the reintroduction of TG inhibition as a therapy for HD may evoke feelings of déjà vu, the outcome this time around could go in a dramatically different direction. | lld:pubmed |
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| pubmed-article:20730854 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20730854 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20730854 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20730854 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20730854 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20730854 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:20730854 | pubmed:issn | 1757-4684 | lld:pubmed |
| pubmed-article:20730854 | pubmed:author | pubmed-author:La... | lld:pubmed |
| pubmed-article:20730854 | pubmed:author | pubmed-author:Kazemi-Esfarj... | lld:pubmed |
| pubmed-article:20730854 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20730854 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:20730854 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20730854 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20730854 | pubmed:pagination | 335-7 | lld:pubmed |
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| pubmed-article:20730854 | pubmed:meshHeading | pubmed-meshheading:20730854... | lld:pubmed |
| pubmed-article:20730854 | pubmed:meshHeading | pubmed-meshheading:20730854... | lld:pubmed |
| pubmed-article:20730854 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20730854 | pubmed:articleTitle | Déjà vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington's disease. | lld:pubmed |
| pubmed-article:20730854 | pubmed:affiliation | Division of Genetics, Department of Pediatrics, University of California, San Diego - La Jolla, CA, USA. | lld:pubmed |
| pubmed-article:20730854 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20730854 | pubmed:publicationType | Comment | lld:pubmed |
| pubmed-article:20730854 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20730854 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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