ReviewAnnual review of biophysics2010
Lessons learned from UvrD helicase: mechanism for directional movement.
Review in Annual review of biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
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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
33 citing papers in PubMed, 50 citations in OpenAlex.
- 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 conserved mechanism for dimerization and activation of superfamily 1A UvrD-family helicases.Nucleic acids research · 2026Article
- The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024Review
- The separation pin distinguishes the pro- and anti-recombinogenic functions of Saccharomyces cerevisiae Srs2.Nature communications · 2023Article
- Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.Methods (San Diego, Calif.) · 2022Review
- Determining translocation orientations of nucleic acid helicases.Methods (San Diego, Calif.) · 2022Review
- Structure-activity relationships at a nucleobase-stacking tryptophan required for chemomechanical coupling in the DNA resecting motor-nuclease AdnAB.Nucleic acids research · 2022Article
- Srs2 and Pif1 as Model Systems for Understanding Sf1a and Sf1b Helicase Structure and Function.Genes · 2021Review
- Clutch mechanism of chemomechanical coupling in a DNA resecting motor nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.Nature communications · 2020Article
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- Interplay between Position-Dependent Codon Usage Bias and Hydrogen Bonding at the 5' End of ORFeomes.mSystems · 2020Article
- Different mechanisms for translocation by monomeric and hexameric helicases.Current opinion in structural biology · 2020Review
- Helicase Mechanisms During Homologous Recombination inAnnual review of biophysics · 2019Review
- Rep and UvrD Antagonize One Another at Stalled Replication Forks and This Is Exacerbated by SSB.ACS omega · 2019Article
- Free-energy simulations reveal molecular mechanism for functional switch of a DNA helicase.eLife · 2018Article
- Real-time imaging of DNA loop extrusion by condensin.Science (New York, N.Y.) · 2018Article
- Structure of mycobacterial 3'-to-5' RNA:DNA helicase Lhr bound to a ssDNA tracking strand highlights distinctive features of a novel family of bacterial helicases.Nucleic acids research · 2018Article
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
How do molecular motors convert chemical energy to mechanical work? Helicases and nucleic acids offer simple motor systems for extensive biochemical and biophysical analyses. Atomic resolution structures of UvrD-like helicases complexed with DNA in the presence of AMPPNP, ADP.Pi, and Pi reveal several salient points that aid our understanding of mechanochemical coupling. Each ATPase cycle causes two motor domains to rotationally close and open. At a minimum, two motor-track contact points of alternating tight and loose attachment convert domain rotations to unidirectional movement. A motor is poised for action only when fully in contact with its track and, if applicable, working against a load. The orientation of domain rotation relative to the track determines whether the movement is linear, spiral, or circular. Motors powered by ATPases likely deliver each power stroke in two parts, before and after ATP hydrolysis. Implications of these findings for analyzing hexameric helicase, F(1)F(0) ATPase, and kinesin are discussed.
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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.