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http://purl.uniprot.org/citations/18990579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18990579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18990579http://www.w3.org/2000/01/rdf-schema#comment"Ribonucleotide reductase (RNR), a crucial enzyme for nucleotide anabolism, is encoded by all living organisms and by large DNA viruses such as the herpesviruses. Surprisingly, the beta-herpesvirus subfamily RNR R1 subunit homologues are catalytically inactive and their function remained enigmatic for many years. Recent work sheds light on the function of M45, the murine cytomegalovirus R1 homologue; during viral evolution, M45 apparently lost its original RNR activity but gained the ability, via inhibiting RIP1, a cellular adaptor protein, to block cellular signaling pathways involved in innate immunity and inflammation. The discovery of this novel mechanism of viral immune subversion provides further support to the concept of evolutionary tinkering."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.org/dc/terms/identifier"doi:10.1016/j.tibs.2008.09.008"xsd:string
http://purl.uniprot.org/citations/18990579http://purl.org/dc/terms/identifier"doi:10.1016/j.tibs.2008.09.008"xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/author"Brune W."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/author"Brune W."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/author"Lembo D."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/author"Lembo D."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/pages"25-32"xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/pages"25-32"xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/title"Tinkering with a viral ribonucleotide reductase."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/title"Tinkering with a viral ribonucleotide reductase."xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/volume"34"xsd:string
http://purl.uniprot.org/citations/18990579http://purl.uniprot.org/core/volume"34"xsd:string
http://purl.uniprot.org/citations/18990579http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18990579
http://purl.uniprot.org/citations/18990579http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18990579
http://purl.uniprot.org/citations/18990579http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18990579
http://purl.uniprot.org/citations/18990579http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18990579
http://purl.uniprot.org/uniprot/P50645http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18990579
http://purl.uniprot.org/uniprot/Q01037http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18990579