| http://purl.uniprot.org/citations/17703232 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17703232 | http://www.w3.org/2000/01/rdf-schema#comment | "Variants of human TRAIL (hTRAIL) and human CD95L (hCD95L), encompassing the TNF homology domain (THD), interact with the corresponding receptors and stimulate CD95 and TRAILR2 signaling after cross-linking. The murine counterparts (mTRAIL, mCD95L) showed no or only low receptor binding and were inactive/poorly active after cross-linking. The stalk region preceding the THD of mCD95L conferred secondary aggregation and restored CD95 activation in the absence of cross-linking. A corresponding variant of mTRAIL, however, was still not able to activate TRAIL death receptors, but gained good activity after cross-linking. Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking. Introduction of the TNC domain also further enhanced the activity of THD encompassing variants of hTRAIL and hCD95L. Thus, spatial fixation of the N-terminus of the THD appears necessary in some TNF ligands to ensure proper receptor binding. This points to yet unanticipated functions of the stalk and/or transmembrane region of TNF ligands for the functionality of these molecules and offers a broadly applicable option to generate recombinant soluble ligands of the TNF family with superior activity."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.cdd.4402213"xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Muller N."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Sebald W."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Pfizenmaier K."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Wajant H."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Berg D."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Siegmund D."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Lehne M."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/author | "Munkel S."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/name | "Cell Death Differ"xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/pages | "2021-2034"xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/title | "Enforced covalent trimerization increases the activity of the TNF ligand family members TRAIL and CD95L."xsd:string |
| http://purl.uniprot.org/citations/17703232 | http://purl.uniprot.org/core/volume | "14"xsd:string |
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