ArticleNature2012
Bypass of a protein barrier by a replicative DNA helicase.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
64 citing papers in PubMed, 96 citations in OpenAlex.
- HSV-1 origin binding protein UL9 forms intermolecular DNA tethers and intramolecular DNA loops.Nature communications · 2026Article
- Article
- A model for polyomavirus helicase activity derived in part from the AlphaFold2 structure of SV40 T-antigen.Journal of virology · 2024Article
- DNA damage-induced phosphorylation of a replicative DNA helicase results in inhibition of DNA replication through attenuation of helicase function.Nucleic acids research · 2024Article
- Single-molecule characterization of SV40 replisome and novel factors: human FPC and Mcm10.Nucleic acids research · 2024Article
- Control of DNA replication in vitro using a reversible replication barrier.Nature protocols · 2024Article
- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins.International journal of molecular sciences · 2024Article
- De novo fabrication of custom-sequence plasmids for the synthesis of long DNA constructs with extrahelical features.Biophysical journal · 2024Article
- Visualizing the dynamics of DNA replication and repair at the single-molecule level.Methods in cell biology · 2024Article
- SV40 T-antigen uses a DNA shearing mechanism to initiate origin unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Transcription-Replication Coordination.Life (Basel, Switzerland) · 2022Review
- Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021Review
- DNA Manipulation and Single-Molecule Imaging.Molecules (Basel, Switzerland) · 2021Review
- Single-Molecule Insights Into the Dynamics of Replicative Helicases.Frontiers in molecular biosciences · 2021Review
- Replication of the Mammalian Genome by Replisomes Specific for Euchromatin and Heterochromatin.Frontiers in cell and developmental biology · 2021Article
- DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021Review
- Duplex DNA engagement and RPA oppositely regulate the DNA-unwinding rate of CMG helicase.Nature communications · 2020Article
- History of DNA Helicases.Genes · 2020Review
- Article
- The Ubiquitin-Specific Protease Usp7, a Novel Merkel Cell Polyomavirus Large T-Antigen Interaction Partner, Modulates Viral DNA Replication.Journal of virology · 2020Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Replicative DNA helicases generally unwind DNA as a single hexamer that encircles and translocates along one strand of the duplex while excluding the complementary strand (known as steric exclusion). By contrast, large T antigen, the replicative DNA helicase of the simian virus 40 (SV40), is reported to function as a pair of stacked hexamers that pumps double-stranded DNA through its central channel while laterally extruding single-stranded DNA. Here we use single-molecule and ensemble assays to show that large T antigen assembled on the SV40 origin unwinds DNA efficiently as a single hexamer that translocates on single-stranded DNA in the 3'-to-5' direction. Unexpectedly, large T antigen unwinds DNA past a DNA-protein crosslink on the translocation strand, suggesting that the large T antigen ring can open to bypass bulky adducts. Together, our data underscore the profound conservation among replicative helicase mechanisms, and reveal a new level of plasticity in the interactions of replicative helicases with DNA damage.
Indexed as
Identifiers
What OpenQuestion holds
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.