ReviewCellular and molecular life sciences : CMLS2010
Polo-box domain: a versatile mediator of polo-like kinase function.
Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
103 citing papers in PubMed, 157 citations in OpenAlex.
- Molecular anatomy of PLK1 master docking motifs.Nature communications · 2026Article
- Bora bridges Aurora-A activation and substrate recognition of PLK1.EMBO reports · 2026Article
- The Role of Aurora Kinase A in HBV-Associated Hepatocellular Carcinomas: A Molecular and Immunohistochemical Study.Diagnostics (Basel, Switzerland) · 2026Article
- Target Binding of Black Phosphorus Nanomaterial to Polo-Like Kinase 1 for Cancer Chemotherapy: A Mutual Selection of Nanomaterial and Protein.Exploration (Beijing, China) · 2025Article
- Review
- Characterization of temperature-sensitive alleles of anillin-like Mid1 and polo kinase Plo1 inmicroPublication biology · 2025Article
- Studying Mitotic Phosphorylation in Drosophila.Methods in molecular biology (Clifton, N.J.) · 2025Article
- PP2A-Tws dephosphorylates Map205, is required for Polo localization to microtubules and promotes cytokinesis in Drosophila.Cell division · 2024Article
- Article
- An acidic loop in the FHA domain of the yeast meiosis-specific kinase Mek1 interacts with a specific motif in a subset of Mek1 substrates.bioRxiv : the preprint server for biology · 2024Article
- Poaceae plants transfer cyclobutane pyrimidine dimer photolyase to chloroplasts for ultraviolet-B resistance.Plant physiology · 2024Article
- Machine learning-informed liquid-liquid phase separation for personalized breast cancer treatment assessment.Frontiers in immunology · 2024Article
- Dissecting the Multiple Functions of the Polo-Like Kinase 1 in the C. elegans Zygote.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Specific inhibition of an anticancer target, polo-like kinase 1, by allosterically dismantling its mechanism of substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 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
- The Role of Polo-Like Kinase 1 in Regulating the Forkhead Box Family Transcription Factors.Cells · 2023Review
- Structural Optimization and Anticancer Activity of Polo-like Kinase 1 (Plk1) Polo-Box Domain (PBD) Inhibitors and Their Prodrugs.ACS pharmacology & translational science · 2023Article
- The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023Review
- Recent Progress on the Localization of PLK1 to the Kinetochore and Its Role in Mitosis.International journal of molecular sciences · 2022Review
43 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
9 authors at 4 institutions in 1 country.
Funding
Abstract
Members of the polo subfamily of protein kinases have emerged as important regulators in diverse aspects of the cell cycle and cell proliferation. A large body of evidence suggests that a highly conserved polo-box domain (PBD) present in the C-terminal non-catalytic region of polo kinases plays a pivotal role in the function of these enzymes. Recent advances in our comprehension of the mechanisms underlying mammalian polo-like kinase 1 (Plk1)-dependent protein-protein interactions revealed that the PBD serves as an essential molecular mediator that brings the kinase domain of Plk1 into proximity with its substrates, mainly through phospho-dependent interactions with its target proteins. In this review, current understanding of the structure and functions of PBD, mode of PBD-dependent interactions and substrate phosphorylation, and other phospho-independent functions of PBD are discussed.
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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.