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http://purl.uniprot.org/citations/24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24844324http://www.w3.org/2000/01/rdf-schema#comment"Degradation of p53 is a cornerstone in the control of its functions as a tumor suppressor. This process is attributed to ubiquitin-dependent modification of p53. In addition to polyubiquitination, we found that p53 is targeted for degradation through ISGylation. Isg15, a ubiquitin-like protein, covalently modifies p53 at 2 sites in the N and C terminus, and ISGylated p53 can be degraded by the 20S proteasome. ISGylation primarily targets a misfolded, dominant-negative p53, and Isg15 deletion in normal cells results in suppression of p53 activity and functions. We propose that Isg15-dependent degradation of p53 represents an alternative mechanism of controlling p53 protein levels, and, thus, it is an attractive pathway for drug discovery."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.org/dc/terms/identifier"doi:10.4161/cc.29209"xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/author"Lane D.P."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/author"Wee S."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/author"Huang Y.F."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/author"Bulavin D.V."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/author"Gunaratne J."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/pages"2200-2210"xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/title"Isg15 controls p53 stability and functions."xsd:string
http://purl.uniprot.org/citations/24844324http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/24844324http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24844324
http://purl.uniprot.org/citations/24844324http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24844324
http://purl.uniprot.org/uniprot/#_A0A0M4B4Y9-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A087WXZ1-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A0C4KX50-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A0C4L134-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A087X1Q1-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A218MJE5-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A087WT22-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A0A0U7X4-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_A0A346XLT4-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324
http://purl.uniprot.org/uniprot/#_D5KL86-mappedCitation-24844324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24844324