pubmed-article:11060309 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0027740 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0007587 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0949610 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C1412925 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:11060309 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:11060309 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:11060309 | pubmed:dateCreated | 2001-5-23 | lld:pubmed |
pubmed-article:11060309 | pubmed:abstractText | Sympathetic neurons undergo protein synthesis-dependent apoptosis when deprived of nerve growth factor (NGF). Expression of SM-20 is up-regulated in NGF-deprived sympathetic neurons, and ectopic SM-20 is sufficient to promote neuronal death in the presence of NGF. We now report that SM-20 is a mitochondrial protein that promotes cell death through a caspase-dependent mechanism. SM-20 immunofluorescence was present in the cytoplasm in a punctate pattern that colocalized with cytochrome oxidase I and with mitochondria-selective dyes. Analysis of SM-20/dihydrofolate reductase fusion proteins revealed that the first 25 amino acids of SM-20 contain a functional mitochondrial targeting sequence. An amino-terminal truncated form of SM-20 was not restricted to mitochondria but instead localized throughout the cytosol and nucleus. Nevertheless, the truncated SM-20 retained the ability to induce neuronal death, similar to the wild type protein. SM-20-induced death was accompanied by caspase-3 activation and was blocked by a general caspase inhibitor. Additionally, overexpression of SM-20, under conditions where cell death is blocked by a general caspase inhibitor, did not result in widespread release of cytochrome c from mitochondria. These results indicate that SM-20 is a novel mitochondrial protein that may be an important mediator of neurotrophin-withdrawal-mediated cell death. | lld:pubmed |
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pubmed-article:11060309 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11060309 | pubmed:language | eng | lld:pubmed |
pubmed-article:11060309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060309 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11060309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11060309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11060309 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11060309 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11060309 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11060309 | pubmed:author | pubmed-author:FreemanR SRS | lld:pubmed |
pubmed-article:11060309 | pubmed:author | pubmed-author:SarmiereP DPD | lld:pubmed |
pubmed-article:11060309 | pubmed:author | pubmed-author:LipscombE AEA | lld:pubmed |
pubmed-article:11060309 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11060309 | pubmed:day | 16 | lld:pubmed |
pubmed-article:11060309 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11060309 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11060309 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11060309 | pubmed:pagination | 5085-92 | lld:pubmed |
pubmed-article:11060309 | pubmed:dateRevised | 2011-9-2 | lld:pubmed |
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pubmed-article:11060309 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11060309 | pubmed:articleTitle | SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons. | lld:pubmed |
pubmed-article:11060309 | pubmed:affiliation | Department of Environmental Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA. | lld:pubmed |
pubmed-article:11060309 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11060309 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11060309 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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