ArticleJournal of molecular biology2021
Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.
Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Structure of an initiation complex of mycobacterial helicase-nuclease AdnAB at a blunt double-strand break reveals local melting that engages the 3' tracking strand at the ratchet pawl of the helicase motor.Nucleic acids research · 2026Article
- Chi hotspot control of RecBCD enzyme requires a RecB tether-RecC groove crosspoint interaction.Genetics · 2026Article
- The Nuclease Domain of E. coli RecBCD Helicase Regulates DNA Binding and Base Pair Melting.Journal of molecular biology · 2026Article
- Subunit Communication within Dimeric SF1 DNA Helicases.Journal of molecular biology · 2024Article
- Communication between DNA and nucleotide binding sites facilitates stepping by the RecBCD helicase.Nucleic acids research · 2024Article
- E. coli RecB Nuclease Domain Regulates RecBCD Helicase Activity but not Single Stranded DNA Translocase Activity.Journal of molecular biology · 2024Article
- RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023Review
- Article
- Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.Methods (San Diego, Calif.) · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
E. coli RecBCD, a helicase/nuclease involved in double stranded (ds) DNA break repair, binds to a dsDNA end and melts out several DNA base pairs (bp) using only its binding free energy. We examined RecBCD-DNA initiation complexes using thermodynamic and structural approaches. Measurements of enthalpy changes for RecBCD binding to DNA ends possessing pre-melted ssDNA tails of increasing length suggest that RecBCD interacts with ssDNA as long as 17-18 nucleotides and can melt at least 10-11 bp upon binding a blunt DNA end. Cryo-EM structures of RecBCD alone and in complex with a blunt-ended dsDNA show significant conformational heterogeneities associated with the RecB nuclease domain (RecB
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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.