| pubmed-article:21326614 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C0022157 | lld:lifeskim |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C1512032 | lld:lifeskim |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C0051380 | lld:lifeskim |
| pubmed-article:21326614 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:21326614 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21326614 | pubmed:dateCreated | 2011-2-17 | lld:pubmed |
| pubmed-article:21326614 | pubmed:abstractText | Gliomas frequently contain mutations in the cytoplasmic NADP(+)-dependent isocitrate dehydrogenase (IDH1) or the mitochondrial NADP(+)-dependent isocitrate dehydrogenase (IDH2). Several different amino acid substitutions recur at either IDH1 R132 or IDH2 R172 in glioma patients. Genetic evidence indicates that these mutations share a common gain of function, but it is unclear whether the shared function is dominant negative activity, neomorphic production of (R)-2-hydroxyglutarate (2HG), or both. | lld:pubmed |
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| pubmed-article:21326614 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21326614 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21326614 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21326614 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21326614 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:YanHaiH | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:YangJianJ | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:BignerDarell... | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:Batinic-Haber... | lld:pubmed |
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| pubmed-article:21326614 | pubmed:author | pubmed-author:SpasojevicIva... | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:JinGenglinG | lld:pubmed |
| pubmed-article:21326614 | pubmed:author | pubmed-author:ReitmanZachar... | lld:pubmed |
| pubmed-article:21326614 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21326614 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:21326614 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21326614 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21326614 | pubmed:pagination | e16812 | lld:pubmed |
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| pubmed-article:21326614 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21326614 | pubmed:articleTitle | 2-hydroxyglutarate production, but not dominant negative function, is conferred by glioma-derived NADP-dependent isocitrate dehydrogenase mutations. | lld:pubmed |
| pubmed-article:21326614 | pubmed:affiliation | The Preston Robert Tisch Brain Tumor Center at Duke, Pediatric Brain Tumor Foundation Institute, and Department of Pathology, Duke University Medical Center, Durham, North Carolina, United States of America. | lld:pubmed |
| pubmed-article:21326614 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21326614 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21326614 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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