ArticleScientific reports2018
Motor-like DNA motion due to an ATP-hydrolyzing protein under nanoconfinement.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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
4 citing papers in PubMed.
- Cas9-Leveraged Single-Molecule Characterization of Sparse Plasmid Vectors in Heterogenous DNA Samples.Applied biochemistry and biotechnology · 2026Article
- Effects of MgBiochemistry and biophysics reports · 2025Article
- Phosphorylated CtIP bridges DNA to promote annealing of broken ends.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Direct observation of confinement-induced diffusophoresis.Nanotechnology · 2019Article
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Authors and funding
8 authors.
Funding
Abstract
We report that long double-stranded DNA confined to quasi-1D nanochannels undergoes superdiffusive motion under the action of the enzyme T4 DNA ligase in the presence of necessary co-factors. Inside the confined environment of the nanochannel, double-stranded DNA molecules stretch out due to self-avoiding interactions. In absence of a catalytically active enzyme, we see classical diffusion of the center of mass. However, cooperative interactions of proteins with the DNA can lead to directed motion of DNA molecules inside the nanochannel. Here we show directed motion in this configuration for three different proteins (T4 DNA ligase, MutS, E. coli DNA ligase) in the presence of their energetic co-factors (ATP, NAD
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