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http://purl.uniprot.org/citations/15518571http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15518571http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15518571http://www.w3.org/2000/01/rdf-schema#comment"The human ribosomal protein S3 (hS3) possesses associated activities that suggest alternative roles beyond its participation in protein translation. For example, it is capable of cleaving apurinic/apyrimidinic (AP) DNA via a beta-elimination reaction, an activity that is missing in partially purified extracts of xeroderma pigmentosum group-D fibroblasts. In a recent study, we showed by surface plasmon resonance (SPR) that hS3 also has a very high apparent binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG) and AP sites in DNA. Using the same SPR technology, it is shown here that hS3 positively interacts with the human base excision repair (BER) enzymes N-glycosylase/AP lyase OGG1 and APE/Ref-1. Using a DNA substrate that allows for the detection of 8-oxoG repair, we also show that hOGG1 N-glycosylase activity becomes increasingly more robust in the presence of hS3. Human S3 was found to co-immunoprecipitate with both hOGG1 and APE/Ref-1, indicating that these proteins physically interact with one another. These results raise the possibility that hS3 not only functions as a ribosomal protein but, in addition, may influence repair activities at sites of DNA damage."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.org/dc/terms/identifier"doi:10.1021/bi049234b"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.org/dc/terms/identifier"doi:10.1021/bi049234b"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Deutsch W.A."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Deutsch W.A."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Hegde V."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/author"Hegde V."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/pages"14211-14217"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/pages"14211-14217"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/title"Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/title"Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/15518571http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/15518571http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15518571
http://purl.uniprot.org/citations/15518571http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15518571
http://purl.uniprot.org/citations/15518571http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15518571
http://purl.uniprot.org/citations/15518571http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15518571