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http://purl.uniprot.org/citations/10346978http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10346978http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10346978http://www.w3.org/2000/01/rdf-schema#comment"A novel member of the interleukin 1 receptor (IL-1R) superfamily, SIGIRR (single Ig IL-1R-related molecule) was identified in mouse and human. Although it shows the typical conserved motifs that characterize the IL-1R and Toll superfamily, it is structurally and functionally distinct from both. SIGIRR has only one Ig domain in its extracellular portion whereas the IL-1R family contains three Ig folds. An unusually long cytoplasmic domain is reminiscent of the structure of drosophila Toll, yet the SIGIRR peptide sequence is more closely related to IL-1RI. The human SIGIRR gene maps to 11p15. 5 and thus is not located in the same cluster on chromosome 2 that is known to contain four members of the IL-1R family. It failed to bind to the known IL-1-family members and, when co-expressed with the IL-1RI, had no effect on the binding of IL-1 and on subsequent nuclear factor kappaB (NFkappaB) activation. A chimera, in which the SIGIRR intracellular domain was fused to the IL-1R extracellular domain, did not activate NFkappaB unlike similar fusion proteins of other IL-1R related molecules. We conclude that the SIGIRR protein represents a novel subtype of the IL-1R superfamily."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.org/dc/terms/identifier"doi:10.1006/cyto.1998.0452"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.org/dc/terms/identifier"doi:10.1006/cyto.1998.0452"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Sims J.E."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Sims J.E."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Thomassen E."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Thomassen E."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Renshaw B.R."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/author"Renshaw B.R."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/name"Cytokine"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/name"Cytokine"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/pages"389-399"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/pages"389-399"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/title"Identification and characterization of SIGIRR, a molecule representing a novel subtype of the IL-1R superfamily."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/title"Identification and characterization of SIGIRR, a molecule representing a novel subtype of the IL-1R superfamily."xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/10346978http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/10346978http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10346978
http://purl.uniprot.org/citations/10346978http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10346978
http://purl.uniprot.org/citations/10346978http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10346978
http://purl.uniprot.org/citations/10346978http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10346978