ArticleMedChemComm2014
Structure-activity relationship studies of SETD8 inhibitors.
Article in MedChemComm, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- SETD8 promotes ovarian clear cell carcinoma by epigenetically activating RNA metabolism genes via H4K20me1.Scientific reports · 2026Article
- SGSS05-NS3, a covalent SETD8 inhibitor that activates p53 pathway in neuroblastoma.Journal of experimental & clinical cancer research : CR · 2025Article
- Multiple functions of the lysine methyltransferase KMT5a in cancer: potential targets for innovative therapies.Clinical epigenetics · 2025Review
- Chemo-proteomics in antimalarial target identification and engagement.Medicinal research reviews · 2023Review
- Drug Discovery Targeting Nuclear Receptor Binding SET Domain Protein 2 (NSD2).Journal of medicinal chemistry · 2023Review
- CDC20 Is Regulated by the Histone Methyltransferase, KMT5A, in Castration-Resistant Prostate Cancer.Cancers · 2023Article
- Total synthesis of nahuoic acid AChemical science · 2021Article
- Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.Nature reviews. Drug discovery · 2021Review
- Enantioselective Synthesis of the Ethyl Analog of the Marine Alkaloid Haliclorensin C.Molecules (Basel, Switzerland) · 2019Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- Development of a Photo-Cross-Linkable Diaminoquinazoline Inhibitor for Target Identification in Plasmodium falciparum.ACS infectious diseases · 2018Article
- Inhibitors of Protein Methyltransferases and Demethylases.Chemical reviews · 2018Review
- Histone lysine methyltransferase structure activity relationships that allow for segregation of G9a inhibition and anti-MedChemComm · 2017Article
- Epigenetic siRNA and Chemical Screens Identify SETD8 Inhibition as a Therapeutic Strategy for p53 Activation in High-Risk Neuroblastoma.Cancer cell · 2017Article
- Turning a Substrate Peptide into a Potent Inhibitor for the Histone Methyltransferase SETD8.ACS medicinal chemistry letters · 2016Article
- Structure-Based Design of a Covalent Inhibitor of the SET Domain-Containing Protein 8 (SETD8) Lysine Methyltransferase.Journal of medicinal chemistry · 2016Article
- Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase.MedChemComm · 2016Article
- Selective inhibitors of protein methyltransferases.Journal of medicinal chemistry · 2015Article
- Synthesis of lysine methyltransferase inhibitors.Frontiers in chemistry · 2015Review
- The emerging role of lysine methyltransferase SETD8 in human diseases.Clinical epigeneticsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
SETD8 (also known as SET8, PR-SET7, or KMT5A (lysine methyltransferase 5A)) is the only known lysine methyltransferase that catalyzes monomethylation of histone H4 lysine 20 (H4K20). In addition to H4K20, SETD8 monomethylates non-histone substrates such as the tumor suppressor p53 and proliferating cell nuclear antigen (PCNA). Because of its role in regulating diverse biological processes, SETD8 has been pursued as a potential therapeutic target. We recently reported the first substrate-competitive SETD8 inhibitor, UNC0379 (
Identifiers
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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.