ArticleThe EMBO journal2010
Rif1 provides a new DNA-binding interface for the Bloom syndrome complex to maintain normal replication.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 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
68 citing papers in PubMed, 100 citations in OpenAlex.
- Chromosome fusion enhances dependency on Rif1 for entanglement resolution during meiosis in S. pombe.Communications biology · 2026Article
- DNA-damage dependent isoform switching modulates RIF1 DNA repair complex assembly and phase separation.The Journal of biological chemistry · 2025Article
- Rif1 Regulates Self-Renewal and Impedes Mesendodermal Differentiation of Mouse Embryonic Stem Cells.Stem cell reviews and reports · 2023Article
- The organizer of chromatin topology RIF1 ensures cellular resilience to DNA replication stress.Life science alliance · 2023Article
- Histone chaperone ASF1 acts with RIF1 to promote DNA end joining in BRCA1-deficient cells.The Journal of biological chemistry · 2022Article
- DNA Double-Strand Breaks as Pathogenic Lesions in Neurological Disorders.International journal of molecular sciences · 2022Review
- Article
- RIF1 acts in DNA repair through phosphopeptide recognition of 53BP1.Molecular cell · 2022Article
- RIF1-ASF1-mediated high-order chromatin structure safeguards genome integrity.Nature communications · 2022Article
- Telomere length regulation by Rif1 protein fromeLife · 2022Article
- SPR Analysis of SUMO-Murine Rap1-Interacting Factor 1 C-Terminal Domain Interaction with G4.Biosensors · 2022Article
- Loss of full-length DNA replication regulator Rif1 in two-cell embryos is associated with zygotic transcriptional activation.The Journal of biological chemistry · 2021Article
- RIF1 Links Replication Timing with Fork Reactivation and DNA Double-Strand Break Repair.International journal of molecular sciences · 2021Review
- Polo-like kinase 1 (Plk1) regulates DNA replication origin firing and interacts with Rif1 in Xenopus.Nucleic acids research · 2021Article
- Fused in sarcoma regulates DNA replication timing and kinetics.The Journal of biological chemistry · 2021Article
- Nuclear organisation and replication timing are coupled through RIF1-PP1 interaction.Nature communications · 2021Article
- Rif1 regulates telomere length through conserved HEAT repeats.Nucleic acids research · 2021Article
- The RIF1-long splice variant promotes G1 phase 53BP1 nuclear bodies to protect against replication stress.eLife · 2020Article
- The role of Rif1 in telomere length regulation is separable from its role in origin firing.eLife · 2020Article
- RIF1 promotes replication fork protection and efficient restart to maintain genome stability.Nature communications · 2019Article
8 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
20 authors at 8 institutions in 3 countries.
Funding
Abstract
BLM, the helicase defective in Bloom syndrome, is part of a multiprotein complex that protects genome stability. Here, we show that Rif1 is a novel component of the BLM complex and works with BLM to promote recovery of stalled replication forks. First, Rif1 physically interacts with the BLM complex through a conserved C-terminal domain, and the stability of Rif1 depends on the presence of the BLM complex. Second, Rif1 and BLM are recruited with similar kinetics to stalled replication forks, and the Rif1 recruitment is delayed in BLM-deficient cells. Third, genetic analyses in vertebrate DT40 cells suggest that BLM and Rif1 work in a common pathway to resist replication stress and promote recovery of stalled forks. Importantly, vertebrate Rif1 contains a DNA-binding domain that resembles the αCTD domain of bacterial RNA polymerase α; and this domain preferentially binds fork and Holliday junction (HJ) DNA in vitro and is required for Rif1 to resist replication stress in vivo. Our data suggest that Rif1 provides a new DNA-binding interface for the BLM complex to restart stalled replication forks.
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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.