ArticleJournal of virology1998
The replication protein A binding site in simian virus 40 (SV40) T antigen and its role in the initial steps of SV40 DNA replication.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
39 citing papers in PubMed, 68 citations in OpenAlex.
- Viruses and the host replisome: discovering oncogenic mechanisms of small DNA tumor viruses.Journal of virology · 2026Review
- Rapid Long-distance Migration of RPA on Single Stranded DNA Occurs Through Intersegmental Transfer Utilizing Multivalent Interactions.Journal of molecular biology · 2024Article
- Review
- Distinct RPA functions promote eukaryotic DNA replication initiation and elongation.Nucleic acids research · 2023Article
- SV40 T antigen helicase domain regions responsible for oligomerisation regulate Okazaki fragment synthesis initiation.FEBS open bio · 2022Article
- Article
- Dynamic elements of replication protein A at the crossroads of DNA replication, recombination, and repair.Critical reviews in biochemistry and molecular biology · 2020Review
- SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication.Nucleic acids research · 2020Article
- Murine polyomavirus DNA transitions through spatially distinct nuclear replication subdomains during infection.PLoS pathogens · 2020Article
- Geminivirus protein structure and function.Molecular plant pathology · 2013Review
- Modeling of the SV40 DNA Replication Machine.Genes · 2012Article
- The structure and function of replication protein A in DNA replication.Sub-cellular biochemistry · 2012Review
- Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.Journal of virology · 2011Article
- A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensable.The Journal of biological chemistry · 2010Article
- Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Functions of alternative replication protein A in initiation and elongation.Biochemistry · 2010Article
- A structure-guided mutational analysis of simian virus 40 large T antigen: identification of surface residues required for viral replication and transformation.Journal of virology · 2009Article
- Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen.Journal of virology · 2008Article
- Timed interactions between viral and cellular replication factors during the initiation of SV40 in vitro DNA replication.The Biochemical journal · 2007Article
- Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication.Journal of virology · 2006Article
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
Abstract
Physical interactions of simian virus 40 (SV40) large tumor (T) antigen with cellular DNA polymerase alpha-primase (Pol/Prim) and replication protein A (RPA) appear to be responsible for multiple functional interactions among these proteins that are required for initiation of viral DNA replication at the origin, as well as during lagging-strand synthesis. In this study, we mapped an RPA binding site in T antigen (residues 164 to 249) that is embedded within the DNA binding domain of T antigen. Two monoclonal antibodies whose epitopes map within this region specifically interfered with RPA binding to T antigen but did not affect T-antigen binding to origin DNA or Pol/Prim, ATPase, or DNA helicase activity and had only a modest effect on origin DNA unwinding, suggesting that they could be used to test the functional importance of this RPA binding site in the initiation of viral DNA replication. To rule out a possible effect of these antibodies on origin DNA unwinding, we used a two-step initiation reaction in which an underwound template was first generated in the absence of primer synthesis. In the second step, primer synthesis was monitored with or without the antibodies. Alternatively, an underwound primed template was formed in the first step, and primer elongation was tested with or without antibodies in the second step. The results show that the antibodies specifically inhibited both primer synthesis and primer elongation, demonstrating that this RPA binding site in T antigen plays an essential role in both events.
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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.