ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural basis for dimerization and activation of UvrD-family helicases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
10 citing papers in PubMed.
- Deleting the 2B domain of mycobacterial UvrD1 unmasks a latent helicase activity in vitro but effaces UvrD1 activity in nucleotide excision repair in vivo.Nucleic acids research · 2026Article
- 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
- FBH1 and RAD54L directly interact and cooperate to drive replication fork reversal.bioRxiv : the preprint server for biology · 2026Article
- A conundrum resolved: regulation and activation of UvrD-family DNA helicases/translocases.Trends in biochemical sciences · 2026Review
- Structural basis for fork reversal and RAD51 regulation by the SCF ubiquitin ligase complex of F-box helicase 1.Nature communications · 2026Article
- The Nuclease Domain of E. coli RecBCD Helicase Regulates DNA Binding and Base Pair Melting.Journal of molecular biology · 2026Article
- The transitional kinetics between open and closed Rep structures can be tuned by salt via two intermediate states.Nucleic acids research · 2026Article
- The herpes simplex origin-binding protein: mechanisms for sequence-specific DNA binding and dimerization revealed by Cryo-EM.Nucleic acids research · 2025Article
- In vivo nucleotide excision repair by mycobacterial UvrD1 requires ATP hydrolysis but does not depend on cysteine disulfide-mediated dimerization and DNA unwinding.Nucleic acids research · 2025Article
Corrections and comments
- Update of
Authors and funding
4 authors.
Funding
Abstract
UvrD-family helicases are superfamily 1A motor proteins that function during DNA replication, recombination, repair, and transcription. UvrD family monomers translocate along single-stranded (ss) DNA but need to be activated by dimerization to unwind DNA in the absence of force or accessory factors. However, prior structural studies have only revealed monomeric complexes. Here, we report the first structures of a dimeric UvrD-family helicase,
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.