ArticleNature communications2026
An information theory approach to quantifying the sequence-dependent response of nucleic acid motors with applications to nanopore DNA sequencing.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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Who cites it
1 citing paper in PubMed.
- HELQ & Hel308: ancient enzymes of DNA repair and recombination.Biochemical Society transactions · 2026Review
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Authors and funding
12 authors.
Funding
Abstract
Motor enzymes that interact with DNA are essential for replicative biological processes. In nanopore sequencing, a motor enzyme controls the motion of a nucleic acid through a protein nanopore, and sequence-dependent blockages of an ion current flowing through the nanopore are used to decode the DNA sequence. The kinetics of these enzymes are sequence-dependent and can serve as an additional source of information during sequencing. Here, we use Mutual Information (MI) to quantify the sequence-dependent kinetics of a Hel308 helicase during nanopore sequencing. We use MI to identify sites in Hel308 that are responsible for sequence-dependent kinetics and develop "k-mer" models of Hel308 kinetics that map kinetics to DNA sequence. We estimate that enzyme kinetics can improve nanopore sequencing accuracy by ~5-fold at high sequencing depth. We mutate Hel308 to identify amino acids involved in DNA translocation and suggest pathways for engineering molecular motors with enhanced responsiveness to DNA sequence.
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Registered trials
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