pubmed-article:11463333 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:11463333 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:11463333 | pubmed:issue | Pt 3 | lld:pubmed |
pubmed-article:11463333 | pubmed:dateCreated | 2001-7-20 | lld:pubmed |
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pubmed-article:11463333 | pubmed:abstractText | The transcription factor nuclear factor kappa B (NF-kappa B) plays a pivotal role in inflammatory processes through induction of adhesion molecules and chemokines. The zinc finger molecule A20 is an important negative regulator of NF-kappa B. The mechanism utilized by A20 is not fully understood, but A20 has been shown to bind to tumour-necrosis-factor-receptor-associated factor (TRAF) molecules, which are necessary for pro-inflammatory cytokine signalling. We report two novel genes, Cezanne (cellular zinc finger anti-NF-kappa B) and TRABID (TRAF-binding domain), with sequence similarity to A20. Co-immunoprecipitation studies indicated that TRAF6 was able to interact with both Cezanne and TRABID. In contrast, reporter gene experiments revealed a specific ability of Cezanne to down-regulate NF-kappa B. It is likely, therefore, that Cezanne participates in the regulation of inflammatory processes. | lld:pubmed |
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pubmed-article:11463333 | pubmed:language | eng | lld:pubmed |
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pubmed-article:11463333 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11463333 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11463333 | pubmed:month | Aug | lld:pubmed |
pubmed-article:11463333 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:KilshawP JPJ | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:EvansP CPC | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:BeyaertRR | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:CoadwellJJ | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:TaylorE RER | lld:pubmed |
pubmed-article:11463333 | pubmed:author | pubmed-author:HeyninckKK | lld:pubmed |
pubmed-article:11463333 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11463333 | pubmed:day | 1 | lld:pubmed |
pubmed-article:11463333 | pubmed:volume | 357 | lld:pubmed |
pubmed-article:11463333 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11463333 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11463333 | pubmed:pagination | 617-23 | lld:pubmed |
pubmed-article:11463333 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:11463333 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11463333 | pubmed:articleTitle | Isolation and characterization of two novel A20-like proteins. | lld:pubmed |
pubmed-article:11463333 | pubmed:affiliation | Molecular Immunology Programme, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK. paul.evans@bbsrc.ac.uk | lld:pubmed |
pubmed-article:11463333 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11463333 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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