ArticleeLife2019
CtIP forms a tetrameric dumbbell-shaped particle which bridges complex DNA end structures for double-strand break repair.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- DNA binding and bridging by human CtIP in the healthy and diseased states.Nucleic acids research · 2024Article
- MEILB2-BRME1 forms a V-shaped DNA clamp upon BRCA2-binding in meiotic recombination.Nature communications · 2024Article
- Article
- New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways.International journal of molecular sciences · 2024Review
- DNA End Joining: G0-ing to the Core.Biomolecules · 2021Review
- Structural basis for the coiled-coil architecture of human CtIP.Open biology · 2021Article
- A fork in the road: Where homologous recombination and stalled replication fork protection part ways.Seminars in cell & developmental biology · 2021Review
- A stapled peptide mimetic of the CtIP tetramerization motif interferes with double-strand break repair and replication fork protection.Science advances · 2021Article
- Phosphorylated CtIP bridges DNA to promote annealing of broken ends.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The internal region of CtIP negatively regulates DNA end resection.Nucleic acids research · 2020Article
- CtIP promotes the motor activity of DNA2 to accelerate long-range DNA end resection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1.PloS one · 2020Article
- Moving Mountains-The BRCA1 Promotion of DNA Resection.Frontiers in molecular biosciences · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
CtIP is involved in the resection of broken DNA during the S and G2 phases of the cell cycle for repair by recombination. Acting with the MRN complex, it plays a particularly important role in handling complex DNA end structures by localised nucleolytic processing of DNA termini in preparation for longer range resection. Here we show that human CtIP is a tetrameric protein adopting a dumbbell architecture in which DNA binding domains are connected by long coiled-coils. The protein complex binds two short DNA duplexes with high affinity and bridges DNA molecules in trans. DNA binding is potentiated by dephosphorylation and is not specific for DNA end structures per se. However, the affinity for linear DNA molecules is increased if the DNA terminates with complex structures including forked ssDNA overhangs and nucleoprotein conjugates. This work provides a biochemical and structural basis for the function of CtIP at complex DNA breaks.
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Registered trials
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