ArticleJournal of virology1996
Amino acids critical for the functions of the bovine papillomavirus type 1 E2 transactivator.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- A Conserved Di-Lysine Motif in the E2 Transactivation Domain Regulates MmuPV1 Replication and Disease Progression.Pathogens (Basel, Switzerland) · 2025Article
- Multiple Roles of Brd4 in the Infectious Cycle of Human Papillomaviruses.Frontiers in molecular biosciences · 2021Review
- Cottontail Rabbit Papillomavirus E1 and E2 Proteins Mutually Influence Their Subcellular Localizations.Journal of virology · 2018Article
- Human Papillomavirus Replication Regulation by Acetylation of a Conserved Lysine in the E2 Protein.Journal of virology · 2018Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Current understanding of the role of the Brd4 protein in the papillomavirus lifecycle.Viruses · 2013Review
- Genetic analysis of the E2 transactivation domain dimerization interface from bovine papillomavirus type 1.Virology · 2013Article
- Acetylation of conserved lysines in bovine papillomavirus E2 by p300.Journal of virology · 2013Article
- Targeting human papillomavirus genome replication for antiviral drug discovery.Antiviral therapy · 2013Review
- The E2 protein of human papillomavirus type 8 increases the expression of matrix metalloproteinase-9 in human keratinocytes and organotypic skin cultures.Medical microbiology and immunology · 2011Article
- Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication.Virology · 2010Article
- Proteasomal degradation of the papillomavirus E2 protein is inhibited by overexpression of bromodomain-containing protein 4.Journal of virology · 2009Article
- Replication and partitioning of papillomavirus genomes.Advances in virus research · 2008Review
- Bromodomain protein 4 mediates the papillomavirus E2 transcriptional activation function.Journal of virology · 2006Article
- The mitotic chromosome binding activity of the papillomavirus E2 protein correlates with interaction with the cellular chromosomal protein, Brd4.Journal of virology · 2005Article
- Conditional mutations in the mitotic chromosome binding function of the bovine papillomavirus type 1 E2 protein.Journal of virology · 2005Article
- Analysis of chromatin attachment and partitioning functions of bovine papillomavirus type 1 E2 protein.Journal of virology · 2004Article
- A transactivator function of cottontail rabbit papillomavirus e2 is essential for tumor induction in rabbits.Journal of virology · 2002Article
- Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the origin.Journal of virology · 1999Article
- Effect of bovine papillomavirus E2 protein-specific monoclonal antibodies on papillomavirus DNA replication.Journal of virology · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal domain of the bovine papillomavirus type 1 E2 protein is important for viral DNA replication, for transcriptional transactivation, and for interaction with the E1 protein. To determine which residues of this 200-amino-acid domain are important for these activities, single conservative amino acid substitutions have been generated in 17 residues that are invariant among all papillomavirus E2 proteins. The resulting mutated E2 proteins were tested for the ability to support viral DNA replication, activate transcription, and cooperatively bind to the origin of replication with the E1 protein. We identified five mutated proteins that were completely defective for transcriptional activation and either were defective or could support viral DNA replication at only low levels. However, several of these proteins could still interact efficiently with the E1 protein. In addition, we identified several mutated proteins that were unable to efficiently cooperatively bind to the origin with the E1 protein. Although a number of the mutated proteins demonstrated wild-type activity in all of the functions tested, only 3 out of 17 mutated viral genomes were able to induce foci in a C127 focus formation assay when the mutations were generated in the background of the entire bovine papillomavirus type 1 genome. This finding suggests that the E2 protein may have additional activities that are important for the viral life cycle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.