http://purl.uniprot.org/citations/20696707 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20696707 | http://www.w3.org/2000/01/rdf-schema#comment | "Cellular FADD-like interleukin-1beta-converting enzyme inhibitory proteins (c-FLIPs; isoforms c-FLIP long [c-FLIP(L)], c-FLIP short [c-FLIP(S)], and c-FLIP Raji [c-FLIP(R)]) regulate caspase-8 activation and death receptor (DR)-induced apoptosis. In this study, using a combination of mathematical modeling, imaging, and quantitative Western blots, we present a new mathematical model describing caspase-8 activation in quantitative terms, which highlights the influence of c-FLIP proteins on this process directly at the CD95 death-inducing signaling complex. We quantitatively define how the stoichiometry of c-FLIP proteins determines sensitivity toward CD95-induced apoptosis. We show that c-FLIP(L) has a proapoptotic role only upon moderate expression in combination with strong receptor stimulation or in the presence of high amounts of one of the short c-FLIP isoforms, c-FLIP(S) or c-FLIP(R). Our findings resolve the present controversial discussion on the function of c-FLIP(L) as a pro- or antiapoptotic protein in DR-mediated apoptosis and are important for understanding the regulation of CD95-induced apoptosis, where subtle differences in c-FLIP concentrations determine life or death of the cells."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.201002060"xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Krammer P.H."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Eils R."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Lavrik I.N."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Beaudouin J."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Richter P."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/author | "Fricker N."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/name | "J Cell Biol"xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/pages | "377-389"xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/title | "Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL."xsd:string |
http://purl.uniprot.org/citations/20696707 | http://purl.uniprot.org/core/volume | "190"xsd:string |
http://purl.uniprot.org/citations/20696707 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20696707 |
http://purl.uniprot.org/citations/20696707 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20696707 |
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