ReviewCell cycle (Georgetown, Tex.)2013
Dbf4: the whole is greater than the sum of its parts.
Review in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- USP48 promotes tumour progression through the deubiquitination and stabilization of DBF4 in clear cell renal carcinoma.Cancer cell international · 2026Article
- Analysis of the response mechanism in lipid degradation of key gene LDH1 knockout strains of Saccharomyces cerevisiae under levulinic acid stress.Archives of microbiology · 2025Article
- Clinical significance and pro-oncogenic function of DBF4 in clear cell renal cell carcinoma.BMC urology · 2025Article
- Genome wide-scale CRISPR-Cas9 knockout screens identify a fitness score for optimized risk stratification in colorectal cancer.Journal of translational medicine · 2024Article
- Efficient, Formal, Material, and Final Causes in Biology and Technology.Entropy (Basel, Switzerland) · 2023Article
- DBF4 Dependent Kinase Inhibition Suppresses Hepatocellular Carcinoma Progression and Potentiates Anti-Programmed Cell Death-1 Therapy.International journal of biological sciences · 2023Article
- Snapshot imprinting as a tool for surface mapping and identification of novel biomarkers of senescent cells.Nanoscale advances · 2022Article
- The interaction between the Dbf4 ortholog Chiffon and Gcn5 is conserved in Dipteran insect species.Insect molecular biology · 2022Article
- Identification and Validation of a Prognostic Model Based on Three MVI-Related Genes in Hepatocellular Carcinoma.International journal of biological sciences · 2022Article
- Article
- Cell-cycle phospho-regulation of the kinetochore.Current genetics · 2021Review
- Fundamental cell cycle kinases collaborate to ensure timely destruction of the synaptonemal complex during meiosis.The EMBO journal · 2017Article
- 'AND' logic gates at work: Crystal structure of Rad53 bound to Dbf4 and Cdc7.Scientific reports · 2016Article
- Characterization of a Drosophila ortholog of the Cdc7 kinase: a role for Cdc7 in endoreplication independent of Chiffon.The Journal of biological chemistry · 2015Article
- A novel non-canonical forkhead-associated (FHA) domain-binding interface mediates the interaction between Rad53 and Dbf4 proteins.The Journal of biological chemistry · 2014Article
- Regulation and roles of Cdc7 kinase under replication stress.Cell cycle (Georgetown, Tex.) · 2014Review
- Human Mesenchymal Stem Cells-mediated Transcriptomic Regulation of Leukemic Cells in Delivering Anti-tumorigenic Effects.Cell transplantationArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Together with cyclin-dependent kinases, the Dbf4-dependent kinase (DDK) is essential to activate the Mcm2-7 helicase and, hence, initiate DNA replication in eukaryotes. Beyond its role as the regulatory subunit of the DDK complex, the Dbf4 protein also regulates the activity of other cell cycle kinases to mediate the checkpoint response and prevent premature mitotic exit under stress. Two features that are unusual in DNA replication proteins characterize Dbf4. The first is its evolutionary divergence; the second is how its conserved motifs are combined to form distinct functional units. This structural plasticity appears to be at odds with the conserved functions of Dbf4. In this review, we summarize recent genetic, biochemical and structural work delineating the multiple interactions mediated by Dbf4 and its various functions during the cell cycle. We also discuss how the limited sequence conservation of Dbf4 may be an advantage to regulate the activities of multiple cell cycle kinases.
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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.