pubmed-article:12374852 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C1333261 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C1423063 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C1149630 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
pubmed-article:12374852 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:12374852 | pubmed:issue | 21 | lld:pubmed |
pubmed-article:12374852 | pubmed:dateCreated | 2002-10-16 | lld:pubmed |
pubmed-article:12374852 | pubmed:abstractText | The SIR2 (silent information regulator 2) gene family has diverse functions in yeast including gene silencing, DNA repair, cell-cycle progression, and chromosome fidelity in meiosis and aging. Human homologues, termed sirtuins, are highly conserved but are of unknown function. We previously identified a large imprinted gene domain on 11p15.5 and investigated the 11p15.5 sirtuin SIRT3. Although this gene was not imprinted, we found that it is localized to mitochondria, with a mitochondrial targeting signal within a unique N-terminal peptide sequence. The encoded protein was found also to possess NAD(+)-dependent histone deacetylase activity. These results suggest a previously unrecognized organelle for sirtuin function and that the role of SIRT3 in mitochondria involves protein deacetylation. | lld:pubmed |
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pubmed-article:12374852 | pubmed:language | eng | lld:pubmed |
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pubmed-article:12374852 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12374852 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12374852 | pubmed:month | Oct | lld:pubmed |
pubmed-article:12374852 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:12374852 | pubmed:author | pubmed-author:BoekeJef DJD | lld:pubmed |
pubmed-article:12374852 | pubmed:author | pubmed-author:FeinbergAndre... | lld:pubmed |
pubmed-article:12374852 | pubmed:author | pubmed-author:OnyangoPatric... | lld:pubmed |
pubmed-article:12374852 | pubmed:author | pubmed-author:McCafferyJ... | lld:pubmed |
pubmed-article:12374852 | pubmed:author | pubmed-author:CelicIvanaI | lld:pubmed |
pubmed-article:12374852 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12374852 | pubmed:day | 15 | lld:pubmed |
pubmed-article:12374852 | pubmed:volume | 99 | lld:pubmed |
pubmed-article:12374852 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12374852 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12374852 | pubmed:pagination | 13653-8 | lld:pubmed |
pubmed-article:12374852 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:12374852 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12374852 | pubmed:articleTitle | SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. | lld:pubmed |
pubmed-article:12374852 | pubmed:affiliation | Institute of Genetic Medicine, Department of Medicine, The Johns Hopkins University School of Medicine, 1064 Ross, 720 Rutland Avenue, Baltimore, MD 21205, USA. | lld:pubmed |
pubmed-article:12374852 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12374852 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12374852 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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