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http://purl.uniprot.org/citations/12840007http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12840007http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12840007http://www.w3.org/2000/01/rdf-schema#comment"Oligonucleosomal fragmentation of chromosomes in dying cells is a hallmark of apoptosis. Little is known about how it is executed or what cellular components are involved. We show that crn-1, a Caenorhabditis elegans homologue of human flap endonuclease-1 (FEN-1) that is normally involved in DNA replication and repair, is also important for apoptosis. Reduction of crn-1 activity by RNA interference resulted in cell death phenotypes similar to those displayed by a mutant lacking the mitochondrial endonuclease CPS-6/endonuclease G. CRN-1 localizes to nuclei and can associate and cooperate with CPS-6 to promote stepwise DNA fragmentation, utilizing the endonuclease activity of CPS-6 and both the 5'-3' exonuclease activity and a previously uncharacterized gap-dependent endonuclease activity of CRN-1. Our results suggest that CRN-1/FEN-1 may play a critical role in switching the state of cells from DNA replication/repair to DNA degradation during apoptosis."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg320"xsd:string
http://purl.uniprot.org/citations/12840007http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg320"xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Shen B."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Shen B."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Yang C."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Yang C."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Xue D."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Xue D."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Parrish J.Z."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/author"Parrish J.Z."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/pages"3451-3460"xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/pages"3451-3460"xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/title"CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/title"CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation."xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12840007http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12840007http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12840007
http://purl.uniprot.org/citations/12840007http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12840007