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http://purl.uniprot.org/citations/16714087http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16714087http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16714087http://www.w3.org/2000/01/rdf-schema#comment"Atrogin-1/MAFbx/FBXO32 is a muscle-specific ubiquitin-ligase (E3) that is dramatically increased in atrophying muscle. Here, we have investigated the functional relationship between atrogin-1 and FBXO25 which shares 65% amino acid identity. Using a RT-PCR, we demonstrated that FBXO25 is highly expressed in brain, kidney, and intestine, whereas atrogin-1 expression is largely restricted to striate muscle. FBXO25 was shown here to contain a functional F-box domain that binds to Skp1 and thereby to Roc1 and Cul1, the major components of SCF-type E3s. In addition, the productive SCF complex containing FBXO25 showed ubiquitin ligase activity. We investigated the differential expression of atrogin-1 and FBXO25 in fasted and dexamethasone-treated mice and also in rats with streptozotocin-induced diabetes. Although the atrogin-1 was strongly induced in muscle in all three models, no changes were observed in the expression of FBXO25. Therefore, here we have shown that FBXO25 is a novel F-box protein analogous to atrogin-1, which is not involved in muscle atrophy. Further functional studies should elucidate the exact role of FBXO25 in the ubiquitin-proteasome pathway."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.org/dc/terms/identifier"doi:10.1016/j.bbagen.2006.03.020"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.org/dc/terms/identifier"doi:10.1016/j.bbagen.2006.03.020"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Baqui M.M."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Baqui M.M."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Gomes M.D."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Gomes M.D."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Maragno A.L."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/author"Maragno A.L."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/pages"966-972"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/pages"966-972"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/title"FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/title"FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle."xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/volume"1760"xsd:string
http://purl.uniprot.org/citations/16714087http://purl.uniprot.org/core/volume"1760"xsd:string
http://purl.uniprot.org/citations/16714087http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16714087
http://purl.uniprot.org/citations/16714087http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16714087
http://purl.uniprot.org/citations/16714087http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16714087
http://purl.uniprot.org/citations/16714087http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16714087