ReviewTrends in biochemical sciences2026
A conundrum resolved: regulation and activation of UvrD-family DNA helicases/translocases.
Review in Trends in biochemical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 2026Article
- A conserved mechanism for dimerization and activation of superfamily 1A UvrD-family helicases.Nucleic acids research · 2026Article
- Biomolecular and cellular chirality: Novel diagnostic perspectives for diseases.APL bioengineering · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Superfamily 1 helicases are conserved nonhexameric ATP-dependent enzymes that unwind DNA and RNA duplexes processively or remove proteins, playing critical roles in DNA repair, replication, recombination, and RNA processing. While crystal structures of Superfamily 1A UvrD-family helicases suggested that monomers are active helicases requiring an essential 2B regulatory domain-DNA interaction, biochemical studies show that helicase activation requires dimerization. Recent cryo-electron microscopy (EM) structures of Mycobacterium tuberculosis UvrD1 dimers reveal that dimerization involves the 2B domains, eliminating their inhibitory interaction with duplex DNA, contradicting these original models. Escherichia coli UvrD dimers use the same dimerization interface, suggesting a general mechanism for this class of helicases. Herein, we describe how these results require re-evaluation of helicase mechanisms that were based on the monomeric structures alone.
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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.