| pubmed-article:16434054 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C1413699 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C1511738 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:16434054 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16434054 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16434054 | pubmed:dateCreated | 2006-3-1 | lld:pubmed |
| pubmed-article:16434054 | pubmed:abstractText | Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome. | lld:pubmed |
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| pubmed-article:16434054 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16434054 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16434054 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16434054 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16434054 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16434054 | pubmed:author | pubmed-author:EnoNN | lld:pubmed |
| pubmed-article:16434054 | pubmed:author | pubmed-author:ParkHyun HoHH | lld:pubmed |
| pubmed-article:16434054 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16434054 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:16434054 | pubmed:volume | 357 | lld:pubmed |
| pubmed-article:16434054 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16434054 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16434054 | pubmed:pagination | 358-64 | lld:pubmed |
| pubmed-article:16434054 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16434054 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16434054 | pubmed:articleTitle | Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly. | lld:pubmed |
| pubmed-article:16434054 | pubmed:affiliation | Department of Biochemistry, Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:16434054 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16434054 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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