ArticleBioorganic & medicinal chemistry letters2017
Characterization of a highly selective inhibitor of the Aurora kinases.
Article in Bioorganic & medicinal chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 15 citations in OpenAlex.
- An AKR1C3-activated kinase inhibitor prodrug.RSC chemical biology · 2026Article
- PHA-680626 Is an Effective Inhibitor of the Interaction between Aurora-A and N-Myc.International journal of molecular sciences · 2021Article
- Structural basis for small molecule targeting of Doublecortin Like Kinase 1 with DCLK1-IN-1.Communications biology · 2021Article
- 7-(2-Anilinopyrimidin-4-yl)-1-benzazepin-2-ones Designed by a "Cut and Glue" Strategy Are Dual Aurora A/VEGF-R Kinase Inhibitors.Molecules (Basel, Switzerland) · 2021Article
- Chemical Biology Toolkit for DCLK1 Reveals Connection to RNA Processing.Cell chemical biology · 2020Article
- Synthesis and Structure-Activity Relationships of DCLK1 Kinase Inhibitors Based on a 5,11-Dihydro-6Journal of medicinal chemistry · 2020Article
- Article
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Authors and funding
7 authors at 5 institutions in 4 countries.
Funding
Abstract
Aurora kinases play an essential role in mitosis and cell cycle regulation. In recent years Aurora kinases have proved popular cancer targets and many inhibitors have been developed. The majority of these clinical candidates are multi-targeted, rendering them inappropriate as tools for studying Aurora kinase mediated signaling. Here we report discovery of a highly selective inhibitor of Aurora kinases A, B and C, with potent cellular activity and minimal off-target activity (PLK4). The X-ray co-crystal structure of Aurora A in complex with compound 2 is reported, and provides insights into the structural determinants of ligand binding and selectivity.
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Registered trials
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