ArticleJournal of virology2000
Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- DNA damage-induced phosphorylation of a replicative DNA helicase results in inhibition of DNA replication through attenuation of helicase function.Nucleic acids research · 2024Article
- Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field.Viruses · 2023Review
- 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
- Article
- Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.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
- Cell cycle regulation of DNA replication.Annual review of genetics · 2007Review
- Stability and function of JC virus large T antigen and T' proteins are altered by mutation of their phosphorylated threonine 125 residues.Journal of virology · 2006Article
- Two heads are better than one: regulation of DNA replication by hexameric helicases.Genes & development · 2004Review
- Interactions required for binding of simian virus 40 T antigen to the viral origin and molecular modeling of initial assembly events.Journal of virology · 2004Article
- Characterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropy.Journal of virology · 2003Article
- Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein.Journal of virology · 2003Article
- Peptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylated.Journal of virology · 2002Article
- Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Molecular and cellular biology · 2002Article
- Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding.Nucleic acids research · 2002Article
- Mutational analysis of simian virus 40 T-antigen primosome activities in viral DNA replication.Journal of virology · 2002Article
- In the simian virus 40 in vitro replication system, start site selection by the polymerase alpha-primase complex is not significantly altered by changes in the concentration of ribonucleotides.Journal of virology · 2001Article
- The simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.Journal of virology · 2000Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Cell cycle-dependent phosphorylation of simian virus 40 (SV40) large tumor antigen (T-ag) on threonine 124 is essential for the initiation of viral DNA replication. A T-ag molecule containing a Thr-->Ala substitution at this position (T124A) was previously shown to bind to the SV40 core origin but to be defective in DNA unwinding and initiation of DNA replication. However, exactly what step in the initiation process is defective as a result of the T124A mutation has not been established. Therefore, to better understand the control of SV40 replication, we have reinvestigated the assembly of T124A molecules on the SV40 origin. Herein it is demonstrated that hexamer formation is unaffected by the phosphorylation state of Thr 124. In contrast, T124A molecules are defective in double-hexamer assembly on subfragments of the core origin containing single assembly units. We also report that T124A molecules are inhibitors of T-ag double hexamer formation. These and related studies indicate that phosphorylation of T-ag on Thr 124 is a necessary step for completing the assembly of functional double hexamers on the SV40 origin. The implications of these studies for the cell cycle control of SV40 DNA replication are discussed.
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