| http://purl.uniprot.org/citations/24816846 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24816846 | http://www.w3.org/2000/01/rdf-schema#comment | "Cellular FLIP (c-FLIP) is an enzymatically inactive paralogue of caspase-8 and as such can block death receptor-induced apoptosis. However, independent of death receptors, c-FLIP-Long (c-FLIPL) can heterodimerize with and activate caspase-8. This is critical for promoting the growth and survival of T lymphocytes as well as the regulation of the RIG-I helicase pathway for type I interferon production in response to viral infections. Truncated forms of FLIP also exist in mammalian cells (c-FLIPS) and certain viruses (v-FLIP), which lack the C-terminal domain that activates caspase-8. Thus, the ratio of c-FLIPL to these short forms of FLIP may greatly influence the outcome of an immune response. We examined this model in mice transgenically expressing c-FLIPS in T cells during infection with Coxsackievirus B3 (CVB3). In contrast to our earlier findings of reduced myocarditis and mortality with CVB3 infection of c-FLIPL-transgenic mice, c-FLIPS-transgenic mice were highly sensitive to CVB3 infection as manifested by increased cardiac virus titers, myocarditis score, and mortality compared to wild-type C57BL/6 mice. This observation was paralleled by a reduction in serum levels of IL-10 and IFN-α in CVB3-infected c-FLIPS mice. In vitro infection of c-FLIPS T cells with CVB3 confirmed these results. Furthermore, molecular studies revealed that following infection of cells with CVB3, c-FLIPL associates with mitochondrial antiviral signaling protein (MAVS), increases caspase-8 activity and type I IFN production, and reduces viral replication, whereas c-FLIPS promotes the opposite phenotype."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0096156"xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Lee S.H."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Jung J.U."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Shi C."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Russell J."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Koenig A."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Roberts B."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Huber S.A."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Budd R.C."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/author | "Buskiewicz I.A."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/pages | "e96156"xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/title | "c-FLIP-Short reduces type I interferon production and increases viremia with coxsackievirus B3."xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://purl.uniprot.org/core/volume | "9"xsd:string |
| http://purl.uniprot.org/citations/24816846 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24816846 |
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| http://purl.uniprot.org/uniprot/#_A0A336TY74-mappedCitation-24816846 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24816846 |
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| http://purl.uniprot.org/uniprot/#_B4E361-mappedCitation-24816846 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24816846 |