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http://purl.uniprot.org/citations/28581483http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28581483http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28581483http://www.w3.org/2000/01/rdf-schema#comment"N-terminal acetylation is an abundant modification influencing protein functions. Because ∼80% of mammalian cytosolic proteins are N-terminally acetylated, this modification is potentially an untapped target for chemical control of their functions. Structural studies have revealed that, like lysine acetylation, N-terminal acetylation converts a positively charged amine into a hydrophobic handle that mediates protein interactions; hence, this modification may be a druggable target. We report the development of chemical probes targeting the N-terminal acetylation-dependent interaction between an E2 conjugating enzyme (UBE2M or UBC12) and DCN1 (DCUN1D1), a subunit of a multiprotein E3 ligase for the ubiquitin-like protein NEDD8. The inhibitors are highly selective with respect to other protein acetyl-amide-binding sites, inhibit NEDD8 ligation in vitro and in cells, and suppress anchorage-independent growth of a cell line with DCN1 amplification. Overall, our data demonstrate that N-terminal acetyl-dependent protein interactions are druggable targets and provide insights into targeting multiprotein E2-E3 ligases."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.org/dc/terms/identifier"doi:10.1038/nchembio.2386"xsd:string
http://purl.uniprot.org/citations/28581483http://purl.org/dc/terms/identifier"doi:10.1038/nchembio.2386"xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Chen T."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Chen T."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Huang G."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Huang G."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Kim H.S."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Kim H.S."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Peng J."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Peng J."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Singh B."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Singh B."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Guy R.K."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Guy R.K."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Schulman B.A."xsd:string
http://purl.uniprot.org/citations/28581483http://purl.uniprot.org/core/author"Schulman B.A."xsd:string