ArticleJournal of virology2004
Interactions required for binding of simian virus 40 T antigen to the viral origin and molecular modeling of initial assembly events.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 26 citations in OpenAlex.
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- Replication of JC Virus DNA in the G144 Oligodendrocyte Cell Line Is Dependent Upon Akt.Journal of virology · 2017Article
- 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
- 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
- Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.Journal of virology · 2011Article
- Simian virus 40 large T antigen can specifically unwind the central palindrome at the origin of DNA replication.Journal of virology · 2009Article
- Evidence for a structural relationship between BRCT domains and the helicase domains of the replication initiators encoded by the Polyomaviridae and Papillomaviridae families of DNA tumor viruses.Journal of virology · 2008Article
- Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.Journal of virology · 2007Article
- Role of the hydrophilic channels of simian virus 40 T-antigen helicase in DNA replication.Journal of virology · 2007Article
- 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.Journal of virology · 2007Article
- The crystal structure of the SV40 T-antigen origin binding domain in complex with DNA.PLoS biology · 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
- Crystal structure of the simian virus 40 large T-antigen origin-binding domain.Journal of virology · 2006Article
- The roles of the residues on the channel beta-hairpin and loop structures of simian virus 40 hexameric helicase.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Two heads are better than one: regulation of DNA replication by hexameric helicases.Genes & development · 2004Review
- The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2.Genes & development · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The purified T-antigen origin binding domain binds site specifically to site II, the central region of the simian virus 40 core origin. However, in the context of full-length T antigen, the origin binding domain interacts poorly with DNA molecules containing just site II. Here we investigate the contributions of additional core origin regions, termed the flanking sequences, to origin recognition and the assembly of T-antigen hexamers and double hexamers. Results from these studies indicate that in addition to site-specific binding of the T-antigen origin binding domain to site II, T-antigen assembly requires non-sequence-specific interactions between a basic finger in the helicase domain and particular flanking sequences. Related studies demonstrate that the assembly of individual hexamers is coupled to the distortions in the proximal flanking sequence. In addition, the point in the double-hexamer assembly process that is regulated by phosphorylation of threonine 124, the sole posttranslational modification required for initiation of DNA replication, was further analyzed. Finally, T-antigen structural information is used to model various stages of T-antigen assembly on the core origin and the regulation of this process.
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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.