ArticleNature communications2024
Structure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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, 13 citations in OpenAlex.
- S-Adenosyl-d-Methionine as a Non-Physiological Substrate for a Wide Range of SAM-Dependent Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- Protein modification systems as cancer biomarkers and therapeutic targets.Precision clinical medicine · 2026Review
- Development of High-Affinity CHD1 Chromodomain Inhibitors.Journal of medicinal chemistry · 2026Article
- Structure-Guided Design of a KMT9 Inhibitor Prodrug with Cellular Activity.Journal of medicinal chemistry · 2025Article
- Overexpression of KMT9α is associated with poor outcome in cholangiocarcinoma patients.Journal of cancer research and clinical oncology · 2025Article
- CytosolicProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lysine Methyltransferase 9 (KMT9) Is an Actionable Target in Muscle-Invasive Bladder Cancer.Cancers · 2024Article
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Authors and funding
21 authors at 2 institutions in 2 countries.
Funding
Abstract
Inhibition of epigenetic regulators by small molecules is an attractive strategy for cancer treatment. Recently, we characterised the role of lysine methyltransferase 9 (KMT9) in prostate, lung, and colon cancer. Our observation that the enzymatic activity was required for tumour cell proliferation identified KMT9 as a potential therapeutic target. Here, we report the development of a potent and selective KMT9 inhibitor (compound 4, KMI169) with cellular activity through structure-based drug design. KMI169 functions as a bi-substrate inhibitor targeting the SAM and substrate binding pockets of KMT9 and exhibits high potency, selectivity, and cellular target engagement. KMT9 inhibition selectively downregulates target genes involved in cell cycle regulation and impairs proliferation of tumours cells including castration- and enzalutamide-resistant prostate cancer cells. KMI169 represents a valuable tool to probe cellular KMT9 functions and paves the way for the development of clinical candidate inhibitors as therapeutic options to treat malignancies such as therapy-resistant prostate cancer.
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