ArticleOncogene1999
Definition of a major p53 binding site on Ad2E1B58K protein and a possible nuclear localization signal on the Ad12E1B54K protein.
Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Identification of Adenovirus E1B-55K Interaction Partners through a Common Binding Motif.Viruses · 2023Article
- Anatomy of Mdm2 and Mdm4 in evolution.Journal of molecular cell biology · 2017Review
- Adenoviral vectors for prodrug activation-based gene therapy for cancer.Anti-cancer agents in medicinal chemistry · 2014Review
- Aggresome formation by the adenoviral protein E1B55K is not conserved among adenovirus species and is not required for efficient degradation of nuclear substrates.Journal of virology · 2013Article
- The WTX tumor suppressor enhances p53 acetylation by CBP/p300.Molecular cell · 2012Article
- Adenovirus type 5 early region 1B 55K oncoprotein-dependent degradation of cellular factor Daxx is required for efficient transformation of primary rodent cells.Journal of virology · 2011Article
- Proteasomal degradation of p53 by human papillomavirus E6 oncoprotein relies on the structural integrity of p53 core domain.PloS one · 2011Article
- Adenovirus E1B 55-kilodalton protein: multiple roles in viral infection and cell transformation.Journal of virology · 2009Review
- The adenoviral E1B 55-kilodalton protein controls expression of immune response genes but not p53-dependent transcription.Journal of virology · 2009Article
- Human telomerase reverse transcriptase promoter-driven oncolytic adenovirus with E1B-19 kDa and E1B-55 kDa gene deletions.Human gene therapy · 2008Article
- Article
- Conditionally replicating adenoviruses for cancer treatment.Current cancer drug targets · 2007Review
- Article
- Sequestration of p53 in the cytoplasm by adenovirus type 12 E1B 55-kilodalton oncoprotein is required for inhibition of p53-mediated apoptosis.Journal of virology · 2003Article
- SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Analyses of single-amino-acid substitution mutants of adenovirus type 5 E1B-55K protein.Journal of virology · 2001Article
- The adenovirus type 5 E1B-55K oncoprotein is a highly active shuttle protein and shuttling is independent of E4orf6, p53 and Mdm2.Oncogene · 2000Article
- Article
- The replicative capacities of large E1B-null group A and group C adenoviruses are independent of host cell p53 status.Journal of virology · 1999Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have established that adenovirus 2/5 early region 1B (Ad E1B) 58K protein binds p53 strongly and co-localizes with it to cytoplasmic dense bodies whilst the homologous Ad12E1B54K protein binds only weakly and co-localizes primarily to the nucleus in Ad12E1 transformed cells. We have used these properties of the E1B proteins from different viral serotypes to map the p53 binding site on the Ad2/5 protein. A set of chimaeric genes was constructed containing different proportions of the Ad12 and Ad2E1B DNA. These, together with Ad12E1A and E1B19K DNA, were transfected into baby rat kidney cells and transformed lines isolated. From an examination of the properties of these Ad12/Ad2E1B fusion proteins in co-immunoprecipitation and subcellular localization experiments it has been concluded that the p53 binding site on Ad2E1B58K protein lies between amino acids 216 and 235 and that the homologous region on Ad12E1B54K protein also binds p53. In addition, a unique nuclear localization signal is located on Ad12E1B54K between residues 228 and 239. We suggest that primary structure differences in these regions of the Ad2 and Ad12E1B proteins are responsible for the different subcellular localizations in AdE1 transformants.
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