{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Teixeira FR"],"funding":["NIGMS NIH HHS"],"pagination":["2746-57"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3034404"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(15)"],"pubmed_abstract":["FBXO25 is one of the 68 human F-box proteins that serve as specificity factors for a family of ubiquitin ligases composed of s-phase-kinase associated protein 1, really interesting new gene-box 1, Cullin 1, and F-box protein (SCF1) that are involved in targeting proteins for destruction across the ubiquitin proteasome system. We recently reported that the FBXO25 protein accumulates in novel subnuclear structures named FBXO25-associated nuclear domains (FAND). Combining two-step affinity purification followed by MS with a classical two-hybrid screen, we identified 132 novel potential FBXO25 interacting partners. One of the identified proteins, beta-actin, physically interacts through its N-terminus with FBXO25 and is enriched in the FBXO25 nuclear compartments. Inhibitors of actin polymeriz"],"journal":["Proteomics"],"pubmed_title":["Identification of FBXO25-interacting proteins using an integrated proteomics approach."],"pmcid":["PMC3034404"],"funding_grant_id":["R01 GM080587","GM 080587","R01 GM080587-01A2"],"pubmed_authors":["Teixeira FR","Kobarg J","Gartner CA","Manfiolli AO","Yokoo S","Baqui MM","de Lanerolle P","Gygi SP","Assmann EM","Maragno AL","Yu H","Gomes MD"],"additional_accession":[]},"is_claimable":false,"name":"Identification of FBXO25-interacting proteins using an integrated proteomics approach.","description":"FBXO25 is one of the 68 human F-box proteins that serve as specificity factors for a family of ubiquitin ligases composed of s-phase-kinase associated protein 1, really interesting new gene-box 1, Cullin 1, and F-box protein (SCF1) that are involved in targeting proteins for destruction across the ubiquitin proteasome system. We recently reported that the FBXO25 protein accumulates in novel subnuclear structures named FBXO25-associated nuclear domains (FAND). Combining two-step affinity purification followed by MS with a classical two-hybrid screen, we identified 132 novel potential FBXO25 interacting partners. One of the identified proteins, beta-actin, physically interacts through its N-terminus with FBXO25 and is enriched in the FBXO25 nuclear compartments. Inhibitors of actin polymeriz","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Aug","modification":"2025-04-22T05:07:43.654Z","creation":"2019-03-27T00:38:44Z"},"accession":"S-EPMC3034404","cross_references":{"pubmed":["20473970"],"doi":["10.1002/pmic.200900419"]}}