ArticleNucleic acids research2008
A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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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Who cites it
78 citing papers in PubMed, 117 citations in OpenAlex.
- Prophase roles of replication protein A in crossover formation and meiotic progression.Journal of microbiology (Seoul, Korea) · 2026Article
- Identification of missense DMC1 variants in males with non-obstructive azoospermia.Journal of assisted reproduction and genetics · 2025Article
- Mei5-Sae3 stabilizes both active and inactive forms of Dmc1 filaments independently of its impact on ATP hydrolysis.Nucleic acids research · 2025Article
- Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Moss BRCA2 lacking the canonical DNA-binding domain promotes homologous recombination and binds to DNA.Nucleic acids research · 2025Article
- Biochemical Mechanisms of Genetic Recombination and DNA Repair.Annual review of biochemistry · 2025Review
- Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination.bioRxiv : the preprint server for biology · 2025Article
- FIGL1 attenuates meiotic interhomolog repair and is counteracted by the RAD51 paralog XRCC2 and the chromosome axis protein ASY1 during meiosis.The New phytologist · 2024Article
- BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode.Nature communications · 2024Article
- RPA interacts with Rad52 to promote meiotic crossover and noncrossover recombination.Nucleic acids research · 2024Article
- A RAD51-ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination.Nature communications · 2023Article
- Repair of DNA double-strand breaks in plant meiosis: role of eukaryotic RecA recombinases and their modulators.Plant reproduction · 2023Review
- Rad51-mediated interhomolog recombination during budding yeast meiosis is promoted by the meiotic recombination checkpoint and the conserved Pif1 helicase.PLoS genetics · 2022Article
- DMC1 attenuates RAD51-mediated recombination in Arabidopsis.PLoS genetics · 2022Article
- Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination.Nucleic acids research · 2021Article
- Guardians of the Genome: BRCA2 and Its Partners.Genes · 2021Review
- Double strand breaks (DSBs) as indicators of genomic instability in PATRR-mediated translocations.Human molecular genetics · 2021Article
- Identification of fidelity-governing factors in human recombinases DMC1 and RAD51 from cryo-EM structures.Nature communications · 2021Article
- High Resolution View on the Regulation of Recombinase Accumulation in Mammalian Meiosis.Frontiers in cell and developmental biology · 2021Review
- Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments ofInternational journal of molecular sciences · 2020Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
The eukaryotic RecA homologs Rad51 and Dmc1 are essential for strand exchange between homologous chromosomes during meiosis. All members of the RecA family of recombinases polymerize on DNA to form helical nucleoprotein filaments, which is the active form of the protein. Here we compare the filament structures of the Rad51 and Dmc1 proteins from both human and budding yeast. Previous studies of Dmc1 filaments suggested that they might be structurally distinct from filaments of other members of the RecA family, including Rad51. The data presented here indicate that Rad51 and Dmc1 filaments are essentially identical with respect to several structural parameters, including persistence length, helical pitch, filament diameter, DNA base pairs per helical turn and helical handedness. These data, together with previous studies demonstrating similar in vitro recombinase activity for Dmc1 and Rad51, support the view that differences in the meiotic function of Rad51 and Dmc1 are more likely to result from the influence of distinct sets of accessory proteins than from intrinsic differences in filament structure.
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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.