{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mallampalli RK"],"funding":["BLRD VA","NHLBI NIH HHS"],"pagination":["5247-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3845358"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["191(10)"],"pubmed_abstract":["Cytokine-driven inflammation underlies the pathobiology of a wide array of infectious and immune-related disorders. The TNFR-associated factor (TRAF) proteins have a vital role in innate immunity by conveying signals from cell surface receptors to elicit transcriptional activation of genes encoding proinflammatory cytokines. We discovered that a ubiquitin E3 ligase F box component, termed Fbxo3, potently stimulates cytokine secretion from human inflammatory cells by mediating the degradation of the TRAF inhibitory protein, Fbxl2. Analysis of the Fbxo3 C-terminal structure revealed that the bacterial-like ApaG molecular signature was indispensible for mediating Fbxl2 disposal and stimulating cytokine secretion. By targeting this ApaG motif, we developed a highly unique, selective genus of s"],"journal":["Journal of immunology (Baltimore, Md. : 1950)"],"pubmed_title":["Targeting F box protein Fbxo3 to control cytokine-driven inflammation."],"pmcid":["PMC3845358"],"funding_grant_id":["I01 BX002200","R01 HL112791","R01 HL116472","R01 HL098174","R01 HL097376","R01 HL01916","R01 HL096376"],"pubmed_authors":["Dunn SR","Glasser JR","Wang C","Coon TA","Chen BB","Weathington NM","Zou C","Mallampalli RK","Zhao J","Zhao Y"],"additional_accession":[]},"is_claimable":false,"name":"Targeting F box protein Fbxo3 to control cytokine-driven inflammation.","description":"Cytokine-driven inflammation underlies the pathobiology of a wide array of infectious and immune-related disorders. The TNFR-associated factor (TRAF) proteins have a vital role in innate immunity by conveying signals from cell surface receptors to elicit transcriptional activation of genes encoding proinflammatory cytokines. We discovered that a ubiquitin E3 ligase F box component, termed Fbxo3, potently stimulates cytokine secretion from human inflammatory cells by mediating the degradation of the TRAF inhibitory protein, Fbxl2. Analysis of the Fbxo3 C-terminal structure revealed that the bacterial-like ApaG molecular signature was indispensible for mediating Fbxl2 disposal and stimulating cytokine secretion. By targeting this ApaG motif, we developed a highly unique, selective genus of s","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2025-04-04T12:27:01.284Z","creation":"2019-03-26T23:43:01Z"},"accession":"S-EPMC3845358","cross_references":{"pubmed":["24123678"],"doi":["10.4049/jimmunol.1300456"]}}