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http://purl.uniprot.org/citations/1445834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1445834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1445834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/1445834http://www.w3.org/2000/01/rdf-schema#comment"Active oxygen species can damage DNA and may play a role in aging and carcinogenesis. We have tested MutY glycosylase for activity on undamaged mispairs as well as mispairs formed with the oxidatively damaged substrates, 8-oxo-7,8-dihydrodeoxyguanine (GO) or 8-oxo-7,8-dihydrodeoxyadenine (AO). MutY acts as a glycosylase on four of the heteroduplexes tested, A/G, A/GO, A/C, and A/AO, removing the undamaged adenine from each substrate. Genetic data suggest that the primary substrate for MutY glycosylase in vivo is the A/GO mispair. We present biochemical evidence demonstrating that MutY glycosylase is an important part of a repair system that includes the MutM and MutT proteins. The GO repair system is dedicated to the repair of the oxidatively damaged guanine and the mutations it can induce."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.org/dc/terms/identifier"doi:10.1021/bi00160a004"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.org/dc/terms/identifier"doi:10.1021/bi00160a004"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Miller J.H."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Miller J.H."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Grollman A.P."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Grollman A.P."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Michaels M.L."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Michaels M.L."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Tchou J."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/author"Tchou J."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/pages"10964-10968"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/pages"10964-10968"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/title"A repair system for 8-oxo-7,8-dihydrodeoxyguanine."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/title"A repair system for 8-oxo-7,8-dihydrodeoxyguanine."xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/1445834http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/1445834http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1445834