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http://purl.uniprot.org/citations/28650317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28650317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28650317http://www.w3.org/2000/01/rdf-schema#comment"ADP-ribosylation (ADPr) is a posttranslational modification (PTM) of proteins that controls many cellular processes, including DNA repair, transcription, chromatin regulation and mitosis. A number of proteins catalyse the transfer and hydrolysis of ADPr, and also specify how and when the modification is conjugated to the targets. We recently discovered a new form of ADPr that is attached to serine residues in target proteins (Ser-ADPr) and showed that this PTM is specifically made by PARP1/HPF1 and PARP2/HPF1 complexes. In this work, we found by quantitative proteomics that histone Ser-ADPr is reversible in cells during response to DNA damage. By screening for the hydrolase that is responsible for the reversal of Ser-ADPr, we identified ARH3/ADPRHL2 as capable of efficiently and specifically removing Ser-ADPr of histones and other proteins. We further showed that Ser-ADPr is a major PTM in cells after DNA damage and that this signalling is dependent on ARH3."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.org/dc/terms/identifier"doi:10.7554/elife.28533"xsd:string
http://purl.uniprot.org/citations/28650317http://purl.org/dc/terms/identifier"doi:10.7554/elife.28533"xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Ahel I."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Ahel I."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Fontana P."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Fontana P."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Matic I."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Matic I."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Bartlett E."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Bartlett E."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Bonfiglio J.J."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Bonfiglio J.J."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Palazzo L."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/author"Palazzo L."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/title"Serine ADP-ribosylation reversal by the hydrolase ARH3."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/title"Serine ADP-ribosylation reversal by the hydrolase ARH3."xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/28650317http://purl.uniprot.org/core/volume"6"xsd:string