ReviewOncogene2015
Understanding the Polo Kinase machine.
Review in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 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
85 citing papers in PubMed, 137 citations in OpenAlex.
- Unraveling systemic responses to NQO1-activated IB-DNQ and Rucaparib single and dual agent therapy in triple-negative breast cancers.bioRxiv : the preprint server for biology · 2025Article
- Fine-tuning probes for fluorescence polarization binding assays of bivalent ligands against polo-like kinase 1 using full-length protein.Bioorganic & medicinal chemistry · 2025Article
- Rational design of potent phosphopeptide binders to endocrine Snk PBD domain by integrating machine learning optimization, molecular dynamics simulation, binding energetics rescoring, and in vitro affinity assay.European biophysics journal : EBJ · 2025Article
- SHCBP1 is a novel regulator of PLK1 phosphorylation and promotes prostate cancer bone metastasis.MedComm · 2025Article
- Dual DNA replication modes: varying fork speeds and initiation rates within the spatial replication program in Xenopus.Nucleic acids research · 2025Article
- PP2A-Tws dephosphorylates Map205, is required for Polo localization to microtubules and promotes cytokinesis in Drosophila.Cell division · 2024Article
- Only InfantInternational journal of molecular sciences · 2024Article
- Affinity enhancement of polo-like kinase 1 polo box domain-binding ligands by a bivalent approach using a covalent kinase-binding component.RSC chemical biology · 2024Article
- Article
- Application of a Fluorescence Recovery-Based Polo-Like Kinase 1 Binding Assay to Polo-Like Kinase 2 and Polo-Like Kinase 3.Biological & pharmaceutical bulletin · 2024Article
- Article
- PLK1 inhibition dampens NLRP3 inflammasome-elicited response in inflammatory disease models.The Journal of clinical investigation · 2023Article
- Genetic enhancers of partial PLK1 inhibition reveal hypersensitivity to kinetochore perturbations.PLoS genetics · 2023Article
- Mechanisms of nuclear pore complex disassembly by the mitotic Polo-like kinase 1 (PLK-1) inScience advances · 2023Article
- Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly inOpen biology · 2023Article
- Onvansertib inhibits the proliferation and improves the cisplatin-resistance of lung adenocarcinoma via β-catenin/c-Myc signaling pathway.American journal of cancer research · 2023Article
- Manipulating the nature of embryonic mitotic waves.Current biology : CB · 2022Article
- Development of ultra-high affinity bivalent ligands targeting the polo-like kinase 1.RSC chemical biology · 2022Article
- HMGA2 expression defines a subset of human AML with immature transcriptional signature and vulnerability to G2/M inhibition.Blood advances · 2022Article
- Oncogenic BRAF induces whole-genome doubling through suppression of cytokinesis.Nature communications · 2022Article
25 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
3 authors at 1 institution in 1 country.
Funding
Abstract
The Polo Kinase is a central regulator of cell division required for several events of mitosis and cytokinesis. In addition to a kinase domain (KD), Polo-like kinases (Plks) comprise a Polo-Box domain (PBD), which mediates protein interactions with targets and regulators of Plks. In all organisms that contain Plks, one Plk family member fulfills several essential functions in the regulation of cell division, and here we refer to this conserved protein as Polo Kinase (Plk1 in humans). The PBD and the KD are capable of both cooperation and mutual inhibition in their functions. Crystal structures of the PBD, the KD and, recently, a PBD-KD complex have helped understanding the inner workings of the Polo Kinase. In parallel, an impressive array of molecular mechanisms has been found to mediate the regulation of the protein. Moreover, the targeting of Polo Kinase in the development of anti-cancer drugs has yielded several molecules with which to chemically modulate Polo Kinase to study its biological functions. Here we review our current understanding of the protein function and regulation of Polo Kinase as a fascinating molecular device in control of cell division.
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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.