{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["DeHart CJ"],"funding":["NIAID NIH HHS","PHS HHS"],"pagination":["1-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3879606"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["The p53 tumor suppressor protein accumulates to very high concentrations in normal human fibroblasts infected by adenovirus type 5 mutants that cannot direct assembly of the viral E1B 55-kDa protein-containing E3 ubiquitin ligase that targets p53 for degradation. Despite high concentrations of nuclear p53, the p53 transcriptional program is not induced in these infected cells. We exploited this system to examine select post-translational modifications (PTMs) present on a transcriptionally inert population of endogenous human p53, as well as on p53 activated in response to etoposide treatment of normal human fibroblasts. These forms of p53 were purified from whole cell lysates by means of immunoaffinity chromatography and SDS-PAGE, and peptides derived from them were subjected to nano-ultra"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Extensive post-translational modification of active and inactivated forms of endogenous p53."],"pmcid":["PMC3879606"],"funding_grant_id":["R56 AI091785","R01AI1058172","R56A111091785","R01 AI058172"],"pubmed_authors":["Chahal JS","Perlman DH","DeHart CJ","Flint SJ"],"additional_accession":[]},"is_claimable":false,"name":"Extensive post-translational modification of active and inactivated forms of endogenous p53.","description":"The p53 tumor suppressor protein accumulates to very high concentrations in normal human fibroblasts infected by adenovirus type 5 mutants that cannot direct assembly of the viral E1B 55-kDa protein-containing E3 ubiquitin ligase that targets p53 for degradation. Despite high concentrations of nuclear p53, the p53 transcriptional program is not induced in these infected cells. We exploited this system to examine select post-translational modifications (PTMs) present on a transcriptionally inert population of endogenous human p53, as well as on p53 activated in response to etoposide treatment of normal human fibroblasts. These forms of p53 were purified from whole cell lysates by means of immunoaffinity chromatography and SDS-PAGE, and peptides derived from them were subjected to nano-ultra","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jan","modification":"2026-05-04T23:54:28.063Z","creation":"2019-03-27T01:19:20Z"},"accession":"S-EPMC3879606","cross_references":{"pubmed":["24056736"],"doi":["10.1074/mcp.M113.030254","10.1074/mcp.m113.030254"]}}