ArticlePloS one2013
Identification and characterization of SMARCAL1 protein complexes.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 31 citations in OpenAlex.
- SMARCAL1 is a candidate therapeutic target for ALT-positive tumors.Genes & development · 2026Article
- Integrated multi-omics analysis revealed that SMARCAL1 serves as an immune related prognostic marker and promotes liver cancer growth via the Hippo/YAP signaling axis.International journal of surgery (London, England) · 2025Article
- S-phase checkpoint protects from aberrant replication fork processing and degradation.Nucleic acids research · 2025Article
- The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA.Nature communications · 2025Article
- Replication stress at microsatellites causes DNA double-strand breaks and break-induced replication.The Journal of biological chemistry · 2020Article
- Advances in understanding DNA processing and protection at stalled replication forks.The Journal of cell biology · 2019Review
- Mechanisms of Oncogene-Induced Replication Stress: Jigsaw Falling into Place.Cancer discovery · 2018Review
- Functions of SMARCAL1, ZRANB3, and HLTF in maintaining genome stability.Critical reviews in biochemistry and molecular biology · 2017Review
- Interactive Roles of DNA Helicases and Translocases with the Single-Stranded DNA Binding Protein RPA in Nucleic Acid Metabolism.International journal of molecular sciences · 2017Review
- SMARCAL1 and telomeres: Replicating the troublesome ends.Nucleus (Austin, Tex.) · 2016Review
- SMARCAL1 maintains telomere integrity during DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The WRN exonuclease domain protects nascent strands from pathological MRE11/EXO1-dependent degradation.Nucleic acids research · 2015Article
- Preventing replication fork collapse to maintain genome integrity.DNA repair · 2015Review
- Smarcal1 promotes double-strand-break repair by nonhomologous end-joining.Nucleic acids research · 2015Article
- High-affinity DNA-binding domains of replication protein A (RPA) direct SMARCAL1-dependent replication fork remodeling.The Journal of biological chemistry · 2015Article
- Replication fork recovery and regulation of common fragile sites stability.Cellular and molecular life sciences : CMLS · 2014Review
- HARP preferentially co-purifies with RPA bound to DNA-PK and blocks RPA phosphorylation.Epigenetics · 2014Article
- Global quantitative modeling of chromatin factor interactions.PLoS computational biology · 2014Article
- Novel SMARCAL1 bi-allelic mutations associated with a chromosomal breakage phenotype in a severe SIOD patient.Journal of clinical immunology · 2014Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
SMARCAL1 is an ATPase in the SNF2 family that functions at damaged replication forks to promote their stability and restart. It acts by translocating on DNA to catalyze DNA strand annealing, branch migration, and fork regression. Many SNF2 enzymes work as motor subunits of large protein complexes. To determine if SMARCAL1 is also a member of a protein complex and to further understand how it functions in the replication stress response, we used a proteomics approach to identify interacting proteins. In addition to the previously characterized interaction with replication protein A (RPA), we found that SMARCAL1 forms complexes with several additional proteins including DNA-PKcs and the WRN helicase. SMARCAL1 and WRN co-localize at stalled replication forks independently of one another. The SMARCAL1 interaction with WRN is indirect and is mediated by RPA acting as a scaffold. SMARCAL1 and WRN act independently to prevent MUS81 cleavage of the stalled fork. Biochemical experiments indicate that both catalyze fork regression with SMARCAL1 acting more efficiently and independently of WRN. These data suggest that RPA brings a complex of SMARCAL1 and WRN to stalled forks, but that they may act in different pathways to promote fork repair and restart.
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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.