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http://purl.uniprot.org/citations/27105115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27105115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27105115http://www.w3.org/2000/01/rdf-schema#comment"Here we report the identification and verification of a β-hydroxybutyrate-derived protein modification, lysine β-hydroxybutyrylation (Kbhb), as a new type of histone mark. Histone Kbhb marks are dramatically induced in response to elevated β-hydroxybutyrate levels in cultured cells and in livers from mice subjected to prolonged fasting or streptozotocin-induced diabetic ketoacidosis. In total, we identified 44 histone Kbhb sites, a figure comparable to the known number of histone acetylation sites. By ChIP-seq and RNA-seq analysis, we demonstrate that histone Kbhb is a mark enriched in active gene promoters and that the increased H3K9bhb levels that occur during starvation are associated with genes upregulated in starvation-responsive metabolic pathways. Histone β-hydroxybutyrylation thus represents a new epigenetic regulatory mark that couples metabolism to gene expression, offering a new avenue to study chromatin regulation and diverse functions of β-hydroxybutyrate in the context of important human pathophysiological states, including diabetes, epilepsy, and neoplasia."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.03.036"xsd:string
http://purl.uniprot.org/citations/27105115http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.03.036"xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Dai L."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Dai L."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Huang H."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Huang H."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Lombard D.B."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Lombard D.B."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Li J.'"xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Li J.'"xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Peng C."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Peng C."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Qi S."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Qi S."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Tan M."xsd:string
http://purl.uniprot.org/citations/27105115http://purl.uniprot.org/core/author"Tan M."xsd:string