ReviewRSC medicinal chemistry2023
Medicinal chemistry approaches to target the MNK-eIF4E axis in cancer.
Review in RSC medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 11 citations in OpenAlex.
- Review
- Article
- Development of a Direct-to-Biology Platform to Discover Potent MNK Inhibitors.Journal of medicinal chemistry · 2026Article
- Inhibitor screening identifies Entecavir as a promising candidate targeting human eIF4E to block cap-dependent translation in cancer: an integrated in silico and in vitro study.Journal of computer-aided molecular design · 2026Article
- Safety and efficacy of the MNK/VEGFR inhibitor JDB153 combined with the anti-PD-1 antibody serplulimab in patients with advanced pancreatic cancer refractory to standard treatment: a single-arm, phase Ib/II study protocol.Frontiers in pharmacology · 2026Article
- Article
- Discovery of Potent and Selective MNK Kinase Inhibitors for the Treatment of Leukemia.Journal of medicinal chemistry · 2025Article
- Design, synthesis and biological evaluation of MNK-PROTACs.Molecular diversity · 2024Article
- Applications of oxetanes in drug discovery and medicinal chemistry.European journal of medicinal chemistry · 2023Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Aberrant translation of proteins that promote cell proliferation is an essential factor that defines oncogenic processes and cancer. The process for ribosomal translation of proteins from mRNA requires an essential initiation step which is controlled by the protein eIF4E, which binds the RNA 5'-cap and forms the eIF4F complex that subsequently translates protein. Typically, eIF4E is activated by phosphorylation on Ser209 by MNK1 and MNK2 kinases. Substantial work has shown that eIF4E and MNK1/2 are dysregulated in many cancers and this axis has therefore become an active area of interest for developing new cancer therapeutics. This review summarizes and discusses recent work to develop small molecules that target different steps in the MNK-eIF4E axis as potential cancer therapeutics. The aim of this review is to cover the breadth of different molecular approaches being taken and the medicinal chemistry basis for their optimization and testing as new cancer therapeutics.
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.