| pubmed-article:12628186 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0079427 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1709130 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1366517 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0068895 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0812204 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1325410 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C0036849 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1442518 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1156189 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1552652 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1552685 | lld:lifeskim |
| pubmed-article:12628186 | lifeskim:mentions | umls-concept:C1705195 | lld:lifeskim |
| pubmed-article:12628186 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12628186 | pubmed:dateCreated | 2003-3-11 | lld:pubmed |
| pubmed-article:12628186 | pubmed:abstractText | Granzyme A (GzmA) induces a caspase-independent cell death pathway characterized by single-stranded DNA nicks and other features of apoptosis. A GzmA-activated DNase (GAAD) is in an ER associated complex containing pp32 and the GzmA substrates SET, HMG-2, and Ape1. We show that GAAD is NM23-H1, a nucleoside diphosphate kinase implicated in suppression of tumor metastasis, and its specific inhibitor (IGAAD) is SET. NM23-H1 binds to SET and is released from inhibition by GzmA cleavage of SET. After GzmA loading or CTL attack, SET and NM23-H1 translocate to the nucleus and SET is degraded, allowing NM23-H1 to nick chromosomal DNA. GzmA-treated cells with silenced NM23-H1 expression are resistant to GzmA-mediated DNA damage and cytolysis, while cells overexpressing NM23-H1 are more sensitive. | lld:pubmed |
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| pubmed-article:12628186 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12628186 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12628186 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12628186 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:12628186 | pubmed:author | pubmed-author:ZhangDongD | lld:pubmed |
| pubmed-article:12628186 | pubmed:author | pubmed-author:FanZusenZ | lld:pubmed |
| pubmed-article:12628186 | pubmed:author | pubmed-author:BeresfordPaul... | lld:pubmed |
| pubmed-article:12628186 | pubmed:author | pubmed-author:LiebermanJudy... | lld:pubmed |
| pubmed-article:12628186 | pubmed:author | pubmed-author:OhDavid YDY | lld:pubmed |
| pubmed-article:12628186 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12628186 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:12628186 | pubmed:volume | 112 | lld:pubmed |
| pubmed-article:12628186 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12628186 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12628186 | pubmed:pagination | 659-72 | lld:pubmed |
| pubmed-article:12628186 | pubmed:dateRevised | 2011-4-25 | lld:pubmed |
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| pubmed-article:12628186 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12628186 | pubmed:articleTitle | Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. | lld:pubmed |
| pubmed-article:12628186 | pubmed:affiliation | Center for Blood Research and Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:12628186 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12628186 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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