| http://purl.uniprot.org/citations/28262558 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28262558 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28262558 | http://www.w3.org/2000/01/rdf-schema#comment | "Methylation of lysine residues on histone tail is a dynamic epigenetic modification that plays a key role in chromatin structure and gene regulation. Members of the KDM5 (also known as JARID1) sub-family are 2-oxoglutarate (2-OG) and Fe2+-dependent oxygenases acting as histone 3 lysine 4 trimethyl (H3K4me3) demethylases, regulating proliferation, stem cell self-renewal, and differentiation. Here we present the characterization of KDOAM-25, an inhibitor of KDM5 enzymes. KDOAM-25 shows biochemical half maximal inhibitory concentration values of <100 nM for KDM5A-D in vitro, high selectivity toward other 2-OG oxygenases sub-families, and no off-target activity on a panel of 55 receptors and enzymes. In human cell assay systems, KDOAM-25 has a half maximal effective concentration of ∼50 μM and good selectivity toward other demethylases. KDM5B is overexpressed in multiple myeloma and negatively correlated with the overall survival. Multiple myeloma MM1S cells treated with KDOAM-25 show increased global H3K4 methylation at transcriptional start sites and impaired proliferation."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.chembiol.2017.02.006"xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.chembiol.2017.02.006"xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Muller S."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Muller S."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Wu N."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Wu N."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Ruda G.F."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Ruda G.F."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Bountra C."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Bountra C."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Fedorov O."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Fedorov O."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Burgess-Brown N.A."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Burgess-Brown N.A."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Oppermann U."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Oppermann U."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Munro S."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "Munro S."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "La Thangue N.B."xsd:string |
| http://purl.uniprot.org/citations/28262558 | http://purl.uniprot.org/core/author | "La Thangue N.B."xsd:string |