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http://purl.uniprot.org/citations/8170954http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8170954http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8170954http://www.w3.org/2000/01/rdf-schema#comment"The tumor-suppressor protein p53 appears to function at the G1 phase of the cell cycle as a checkpoint in response to DNA damage. Mutations in the p53 gene lead to an increased rate of genomic instability and tumorigenesis. The E2F-1 transcription factor is a protein partner of the retinoblastoma-susceptibility gene product, RB. E2F-1 appears to function as a positive regulator or signal for entry into S phase. To explore possible interactions of p53 and E2F-1 in the cell cycle, a human E2F-1 expression plasmid was introduced into a murine cell line containing a temperature-sensitive p53 allele which produces a p53 protein in the wild-type conformation at 32 degrees C and the mutant form at 37.5 degrees C. Coexpression of the wild-type p53 protein and E2F-1 in these cells resulted in a rapid loss of cell viability through a process of apoptosis. Thus, the cell cycle utilizes an interacting or communicative pathway between RB-E2F-1 and p53."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.org/dc/terms/identifier"doi:10.1073/pnas.91.9.3602"xsd:string
http://purl.uniprot.org/citations/8170954http://purl.org/dc/terms/identifier"doi:10.1073/pnas.91.9.3602"xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/author"Levine A.J."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/author"Levine A.J."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/pages"3602-3606"xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/pages"3602-3606"xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/title"P53 and E2F-1 cooperate to mediate apoptosis."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/title"P53 and E2F-1 cooperate to mediate apoptosis."xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/8170954http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/8170954http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8170954
http://purl.uniprot.org/citations/8170954http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8170954
http://purl.uniprot.org/citations/8170954http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8170954
http://purl.uniprot.org/citations/8170954http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8170954
http://purl.uniprot.org/uniprot/Q01094http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8170954
http://purl.uniprot.org/uniprot/Q01094#attribution-EAAC649808635B273CB73EC99E8BABABhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8170954