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http://purl.uniprot.org/SHA-384/F7292E138168D8385985D39B78713C6014C9039C140F71F408EE87016F3B780F6F5F691A4CFE7472141533E72794CC36http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/F7292E138168D8385985D39B78713C6014C9039C140F71F408EE87016F3B780F6F5F691A4CFE7472141533E72794CC36http://www.w3.org/2000/01/rdf-schema#comment"we showed that CHK2-dependent phosphorylation of PARP1 not only regulates its cellular localization but also promotes its catalytic activity and its interaction with XRCC1. These findings indicate that CHK2 exerts a multifaceted impact on PARP1 in response to oxidative stress to facilitate DNA repair and to maintain cell survival."xsd:string
http://purl.uniprot.org/uniprot/#_53AF1F67A55058F796071415DF04A4ED5FF998D44CC9B1712D984E9D1365D0911041E00F5C99D8965262DD812712499Bhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/F7292E138168D8385985D39B78713C6014C9039C140F71F408EE87016F3B780F6F5F691A4CFE7472141533E72794CC36
http://purl.uniprot.org/uniprot/Q59HH7http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F7292E138168D8385985D39B78713C6014C9039C140F71F408EE87016F3B780F6F5F691A4CFE7472141533E72794CC36
http://purl.uniprot.org/uniprot/#_Q59HH7-mappedCitation-30254210http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/F7292E138168D8385985D39B78713C6014C9039C140F71F408EE87016F3B780F6F5F691A4CFE7472141533E72794CC36