| pubmed-article:12446564 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1335623 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1538842 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1415715 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1150524 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1522240 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12446564 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:12446564 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:12446564 | pubmed:dateCreated | 2002-12-11 | lld:pubmed |
| pubmed-article:12446564 | pubmed:abstractText | RIP1 and its homologs, RIP2 and RIP3, form part of a family of Ser/Thr kinases that regulate signal transduction processes leading to NF-kappa B activation. Here, we identify RIP4 (DIK/PKK) as a novel member of the RIP kinase family. RIP4 contains an N-terminal RIP-like kinase domain and a C-terminal region characterized by the presence of 11 ankyrin repeats. Overexpression of RIP4 leads to activation of NF-kappa B and JNK. Kinase inactive RIP4 or a truncated version containing the ankyrin repeats have a dominant negative (DN) effect on NF-kappa B induction by multiple stimuli. RIP4 binds to several members of the TRAF protein family, and DN versions of TRAF1, TRAF3 and TRAF6 inhibit RIP4-induced NF-kappa B activation. Moreover, RIP4 is cleaved after Asp340 and Asp378 during Fas-induced apoptosis. These data suggest that RIP4 is involved in NF-kappa B and JNK signaling and that caspase-dependent processing of RIP4 may negatively regulate NF-kappa B-dependent pro-survival or pro-inflammatory signals. | lld:pubmed |
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| pubmed-article:12446564 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12446564 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12446564 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12446564 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12446564 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12446564 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12446564 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12446564 | pubmed:issn | 1469-221X | lld:pubmed |
| pubmed-article:12446564 | pubmed:author | pubmed-author:TschoppJürgJ | lld:pubmed |
| pubmed-article:12446564 | pubmed:author | pubmed-author:ThomeMargotM | lld:pubmed |
| pubmed-article:12446564 | pubmed:author | pubmed-author:MartinonFabio... | lld:pubmed |
| pubmed-article:12446564 | pubmed:author | pubmed-author:MeylanEtienne... | lld:pubmed |
| pubmed-article:12446564 | pubmed:author | pubmed-author:GschwendtMich... | lld:pubmed |
| pubmed-article:12446564 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12446564 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:12446564 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12446564 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12446564 | pubmed:pagination | 1201-8 | lld:pubmed |
| pubmed-article:12446564 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
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| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:meshHeading | pubmed-meshheading:12446564... | lld:pubmed |
| pubmed-article:12446564 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12446564 | pubmed:articleTitle | RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-kappa B and is processed during apoptosis. | lld:pubmed |
| pubmed-article:12446564 | pubmed:affiliation | Institute of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, CH-1066 Epalinges, Switzerland. | lld:pubmed |
| pubmed-article:12446564 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12446564 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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