| pubmed-article:18264101 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C1155065 | lld:lifeskim |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C1416991 | lld:lifeskim |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C1554080 | lld:lifeskim |
| pubmed-article:18264101 | lifeskim:mentions | umls-concept:C1706198 | lld:lifeskim |
| pubmed-article:18264101 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18264101 | pubmed:dateCreated | 2008-2-20 | lld:pubmed |
| pubmed-article:18264101 | pubmed:abstractText | The paracaspase MALT1 is pivotal in antigen receptor-mediated lymphocyte activation and lymphomagenesis. MALT1 contains a caspase-like domain, but it is unknown whether this domain is proteolytically active. Here we report that MALT1 had arginine-directed proteolytic activity that was activated after T cell stimulation, and we identify the signaling protein Bcl-10 as a MALT1 substrate. Processing of Bcl-10 after Arg228 was required for T cell receptor-induced cell adhesion to fibronectin. In contrast, MALT1 activity but not Bcl-10 cleavage was essential for optimal activation of transcription factor NF-kappaB and production of interleukin 2. Thus, the proteolytic activity of MALT1 is central to T cell activation, which suggests a possible target for the development of immunomodulatory or anticancer drugs. | lld:pubmed |
| pubmed-article:18264101 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18264101 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18264101 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18264101 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18264101 | pubmed:issn | 1529-2916 | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:ThomeMargotM | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:RuferNathalie... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:FaselNicolasN | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:GaideOlivierO | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:RuedaDanielD | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:HailfingerSte... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:TapernouxMyri... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:IancuEmanuela... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:RebeaudFabien... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:GuzzardiMonts... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:Posevitz-Fejf... | lld:pubmed |
| pubmed-article:18264101 | pubmed:author | pubmed-author:MoserRogerR | lld:pubmed |
| pubmed-article:18264101 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18264101 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:18264101 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18264101 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18264101 | pubmed:pagination | 272-81 | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
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| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:meshHeading | pubmed-meshheading:18264101... | lld:pubmed |
| pubmed-article:18264101 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18264101 | pubmed:articleTitle | The proteolytic activity of the paracaspase MALT1 is key in T cell activation. | lld:pubmed |
| pubmed-article:18264101 | pubmed:affiliation | Department of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland. | lld:pubmed |
| pubmed-article:18264101 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18264101 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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