ArticleBioorganic & medicinal chemistry2013
Development of cyclic peptomer inhibitors targeting the polo-box domain of polo-like kinase 1.
Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 42 citations in OpenAlex.
- An mRNA Display Approach for Covalent Targeting of aJournal of the American Chemical Society · 2025Article
- Identification of Covalent Cyclic Peptide Inhibitors Targeting Protein-Protein Interactions Using Phage Display.Journal of the American Chemical Society · 2025Article
- Identification of Covalent Cyclic Peptide Inhibitors Targeting Protein-Protein Interactions Using Phage Display.bioRxiv : the preprint server for biology · 2024Article
- An mRNA Display Approach for Covalent Targeting of abioRxiv : the preprint server for biology · 2024Article
- Novel Macrocyclic Peptidomimetics Targeting the Polo-Box Domain of Polo-Like Kinase 1.Journal of medicinal chemistry · 2022Article
- Recent Trends in Cyclic Peptides as Therapeutic Agents and Biochemical Tools.Biomolecules & therapeutics · 2020Review
- A Rapid and Efficient Building Block Approach for Click Cyclization of Peptoids.Frontiers in chemistry · 2020Article
- Histidine N(τ)-cyclized macrocycles as a new genre of polo-like kinase 1 polo-box domain-binding inhibitors.Bioorganic & medicinal chemistry letters · 2018Article
- Targeting kinase signaling pathways with constrained peptide scaffolds.Pharmacology & therapeutics · 2017Review
- Current progress and future perspectives in the development of anti-polo-like kinase 1 therapeutic agents.F1000Research · 2017Review
- Application of oxime-diversification to optimize ligand interactions within a cryptic pocket of the polo-like kinase 1 polo-box domain.Bioorganic & medicinal chemistry letters · 2016Article
- DNA Three Way Junction Core Decorated with Amino Acids-Like Residues-Synthesis and Characterization.Molecules (Basel, Switzerland) · 2016Article
- Recent Advances and New Strategies in Targeting Plk1 for Anticancer Therapy.Trends in pharmacological sciences · 2015Review
- Neighbor-directed histidine N (τ)-alkylation: A route to imidazolium-containing phosphopeptide macrocycles.Biopolymers · 2015Article
- Structural basis for recognition of Emi2 by Polo-like kinase 1 and development of peptidomimetics blocking oocyte maturation and fertilization.Scientific reports · 2015Article
- Article
- Design and synthesis of a cell-permeable, drug-like small molecule inhibitor targeting the polo-box domain of polo-like kinase 1.PloS one · 2014Article
- Article
- Putting a bit into the polo-box domain of polo-like kinase 1.Journal of analytical science and technologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
Abstract
The polo-box domain (PBD) of polo-like kinase 1 (Plk1) is essentially required for the function of Plk1 in cell proliferation. The availability of the phosphopeptide-binding pocket on PBD provides a unique opportunity to develop novel protein-protein interaction inhibitors. Recent identification of a minimal 5-residue-long phosphopeptide, PLHSpT, as a Plk1 PBD-specific ligand has led to the development of several peptide-based inhibitors, but none of them is cyclic peptide. Through the combination of single-peptoid mimics and thio-ether bridged cyclization, we successfully demonstrated for the first time two cyclic peptomers, PL-116 and PL-120, dramatically improved the binding affinity without losing mono-specificity against Plk1 PBD in comparison with the linear parental peptide, PLHSpT. These cyclic peptomers could serve as promising templates for future drug designs to inhibit Plk1 PBD.
Indexed as
Identifiers
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.