{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Rask GC"],"funding":["NCI NIH HHS"],"pubmed_abstract":["Genes encoding the RNA-binding proteins FUS, EWSR1, and TAF15 (FET proteins) are involved in chromosomal translocations in rare sarcomas. FET-rearranged sarcomas are often aggressive malignancies affecting patients of all ages. New therapies are needed. These translocations fuse the 5' portion of the FET gene with a 3' partner gene encoding a transcription factor (TF). The resulting fusion proteins are oncogenic TFs with a FET protein low complexity domain (LCD) and a DNA binding domain. FET fusion proteins have proven stubbornly difficult to target directly and promising strategies target critical co-regulators. One candidate is lysine specific demethylase 1 (LSD1). LSD1 is recruited by multiple FET fusions, including EWSR1::FLI1. LSD1 promotes EWSR1::FLI1 activity and treatment with the "],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.05.19.594897"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11142045"],"repository":["biostudies-literature"],"pubmed_title":["Seclidemstat blocks the transcriptional function of multiple FET-fusion oncoproteins."],"pmcid":["PMC11142045"],"funding_grant_id":["T32 CA269052"],"pubmed_authors":["Cannon MV","Taslim C","Theisen ER","Bayanjargal A","Selich-Anderson J","Duncan A","Crow JC","Rask GC"],"additional_accession":[]},"is_claimable":false,"name":"Seclidemstat blocks the transcriptional function of multiple FET-fusion oncoproteins.","description":"Genes encoding the RNA-binding proteins FUS, EWSR1, and TAF15 (FET proteins) are involved in chromosomal translocations in rare sarcomas. FET-rearranged sarcomas are often aggressive malignancies affecting patients of all ages. New therapies are needed. These translocations fuse the 5' portion of the FET gene with a 3' partner gene encoding a transcription factor (TF). The resulting fusion proteins are oncogenic TFs with a FET protein low complexity domain (LCD) and a DNA binding domain. FET fusion proteins have proven stubbornly difficult to target directly and promising strategies target critical co-regulators. One candidate is lysine specific demethylase 1 (LSD1). LSD1 is recruited by multiple FET fusions, including EWSR1::FLI1. LSD1 promotes EWSR1::FLI1 activity and treatment with the ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-05-29T03:15:03.065Z","creation":"2026-05-29T03:06:41.893Z"},"accession":"S-EPMC11142045","cross_references":{"pubmed":["38826330"],"doi":["10.1101/2024.05.19.594897"]}}