ArticleAnalytical chemistry2018
Application of Electrochemical Devices to Characterize the Dynamic Actions of Helicases on DNA.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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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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
7 citing papers in PubMed, 8 citations in OpenAlex.
- A Robust Equivalent Circuit Model for DNA-Mediated Electrochemistry.ChemPlusChem · 2026Article
- Molecular Characterization of Helicase and Nuclease Domains in PPV5 NS1 from Mexican Full-Length Sequence.Viruses · 2026Article
- Integrating Structural, Biochemical, and Cellular Perspectives on the TFIIH Helicases XPB and XPD.Biomolecules · 2026Review
- Molecular wrench activity of DNA helicases: Keys to modulation of rapid kinetics in DNA repair.Protein science : a publication of the Protein Society · 2023Article
- Structural basis of the XPB helicase-Bax1 nuclease complex interacting with the repair bubble DNA.Nucleic acids research · 2020Article
- Structural basis of the XPB-Bax1 complex as a dynamic helicase-nuclease machinery for DNA repair.Nucleic acids research · 2020Article
- Structural Basis for S100B Interaction with its Target Proteins.Journal of molecular and genetic medicine : an international journal of biomedical research · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Much remains to be understood about the kinetics and thermodynamics of DNA helicase binding and activity. Here, we utilize probe-modified DNA monolayers on multiplexed gold electrodes as a sensitive recognition element and morphologically responsive transducer of helicase-DNA interactions. The electrochemical signals from these devices are highly sensitive to structural distortion of the DNA produced by the helicases. We used this DNA electrochemistry to distinguish the details of the DNA interactions of three distinct XPB helicases, which belong to the superfamily-2 of helicases. Clear changes in DNA melting temperature and duplex stability were observed upon helicase binding, shifts that could not be observed with conventional UV-visible absorption measurements. Binding dissociation constants were estimated in the range from 10 to 50 nM and correlated with observations of activity. ATP-stimulated DNA unwinding activity was also followed, revealing exponential time scales and distinct time constants associated with conventional and molecular wrench modes of operation further confirmed by crystal structures. These devices thus provide a sensitive measure of the structural thermodynamics and kinetics of helicase-DNA interactions.
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Registered trials
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