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http://purl.uniprot.org/citations/6371006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/author"Breimer L.H."xsd:string
http://purl.uniprot.org/citations/6371006http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6371006
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/title"DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli."xsd:string
http://purl.uniprot.org/citations/6371006http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)91047-1"xsd:string
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/author"Lindahl T."xsd:string
http://purl.uniprot.org/uniprot/P0AB83#attribution-EB7D784BA46CA11DE9827E48D9199641http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6371006
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/pages"5543-5548"xsd:string
http://purl.uniprot.org/citations/6371006http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6371006
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/uniprot/P0AB83http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6371006
http://purl.uniprot.org/citations/6371006http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/uniprot/#_P0AB83-citation-6371006http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6371006