ArticleJournal of virology2007
Model for T-antigen-dependent melting of the simian virus 40 core origin based on studies of the interaction of the beta-hairpin with DNA.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 31 citations in OpenAlex.
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- Unlicensed origin DNA melting by MCV and SV40 polyomavirus LT proteins is independent of ATP-dependent helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Replication of JC Virus DNA in the G144 Oligodendrocyte Cell Line Is Dependent Upon Akt.Journal of virology · 2017Article
- Review
- Article
- Structural Based Analyses of the JC Virus T-Antigen F258L Mutant Provides Evidence for DNA Dependent Conformational Changes in the C-Termini of Polyomavirus Origin Binding Domains.PLoS pathogens · 2016Article
- Article
- Sequence comparison and phylogenetic analysis by the Maximum Likelihood method of ribosome-inactivating proteins from angiosperms.Plant molecular biology · 2014Article
- Insights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domain.PLoS pathogens · 2014Article
- Mechanism of origin DNA recognition and assembly of an initiator-helicase complex by SV40 large tumor antigen.Cell reports · 2013Article
- Analysis of the costructure of the simian virus 40 T-antigen origin binding domain with site I reveals a correlation between GAGGC spacing and spiral assembly.Journal of virology · 2013Article
- Modeling of the SV40 DNA Replication Machine.Genes · 2012Article
- ATP-dependent conformational dynamics underlie the functional asymmetry of the replicative helicase from a minimalist eukaryote.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain.Acta crystallographica. Section D, Biological crystallography · 2011Article
- The structural basis for MCM2-7 helicase activation by GINS and Cdc45.Nature structural & molecular biology · 2011Article
- Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.Journal of virology · 2011Article
- Origin DNA melting and unwinding in DNA replication.Current opinion in structural biology · 2010Review
- Conformational rearrangements of SV40 large T antigen during early replication events.Journal of molecular biology · 2010Article
- Residues in the central beta-hairpin of the DNA helicase of bacteriophage T7 are important in DNA unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication.Virology · 2010Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The interaction of simian virus 40 (SV40) T antigen (T-ag) with the viral origin has served as a model for studies of site-specific recognition of a eukaryotic replication origin and the mechanism of DNA unwinding. These studies have revealed that a motif termed the "beta-hairpin" is necessary for assembly of T-ag on the SV40 origin. Herein it is demonstrated that residues at the tip of the "beta-hairpin" are needed to melt the origin-flanking regions and that the T-ag helicase domain selectively assembles around one of the newly generated single strands in a manner that accounts for its 3'-to-5' helicase activity. Furthermore, T-ags mutated at the tip of the "beta-hairpin" are defective for oligomerization on duplex DNA; however, they can assemble on hybrid duplex DNA or single-stranded DNA (ssDNA) substrates provided the strand containing the 3' extension is present. Collectively, these experiments indicate that residues at the tip of the beta-hairpin generate ssDNA in the core origin and that the ssDNA is essential for subsequent oligomerization 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.