ArticleJournal of medicinal chemistry2013
Small-molecule ligands of methyl-lysine binding proteins: optimization of selectivity for L3MBTL3.
Article in Journal of medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 65 citations in OpenAlex.
- An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering.Nature communications · 2023Article
- Chemical tools targeting readers of lysine methylation.Current opinion in chemical biology · 2023Review
- The structure, binding and function of a Notch transcription complex involving RBPJ and the epigenetic reader protein L3MBTL3.Nucleic acids research · 2022Article
- Polymer-supported synthesis ofRSC advances · 2021Article
- Epigenetic Modulators as Potential Multi-targeted Drugs Against Hedgehog Pathway for Treatment of Cancer.The protein journal · 2019Article
- Palladium-Catalyzed Hydroxycarbonylation of (Hetero)aryl Halides for DNA-Encoded Chemical Library Synthesis.Bioconjugate chemistry · 2019Article
- Targeting epigenetic modifications in cancer therapy: erasing the roadmap to cancer.Nature medicine · 2019Review
- Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4The Journal of biological chemistry · 2019Article
- RNA-modifying proteins as anticancer drug targets.Nature reviews. Drug discovery · 2018Review
- Identification of ten variants associated with risk of estrogen-receptor-negative breast cancer.Nature genetics · 2017Article
- Palladium-Catalyzed Decarboxylative Ortho-Acylation of Tertiary Benzamides with Arylglyoxylic Acids.ACS omega · 2017Article
- A chemical probe toolbox for dissecting the cancer epigenome.Nature reviews. Cancer · 2017Review
- Structure-Activity Relationships and Kinetic Studies of Peptidic Antagonists of CBX Chromodomains.Journal of medicinal chemistry · 2016Article
- Review
- Chemical probes for methyl lysine reader domains.Current opinion in chemical biology · 2016Review
- Epigenetics: A primer for clinicians.Blood reviews · 2016Review
- Histone Modifications and Cancer.Cold Spring Harbor perspectives in biology · 2016Review
- The L3MBTL3 Methyl-Lysine Reader Domain Functions As a Dimer.ACS chemical biology · 2016Article
- Selective Inhibition of CBX6: A Methyllysine Reader Protein in the Polycomb Family.ACS medicinal chemistry letters · 2016Article
- Targeting epigenetic regulations in cancer.Acta biochimica et biophysica Sinica · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Lysine methylation is a key epigenetic mark, the dysregulation of which is linked to many diseases. Small-molecule antagonism of methyl-lysine (Kme) binding proteins that recognize such epigenetic marks can improve our understanding of these regulatory mechanisms and potentially validate Kme binding proteins as drug-discovery targets. We previously reported the discovery of 1 (UNC1215), the first potent and selective small-molecule chemical probe of a methyl-lysine reader protein, L3MBTL3, which antagonizes the mono- and dimethyl-lysine reading function of L3MBTL3. The design, synthesis, and structure-activity relationship studies that led to the discovery of 1 are described herein. These efforts established the requirements for potent L3MBTL3 binding and enabled the design of novel antagonists, such as compound 2 (UNC1679), that maintain in vitro and cellular potency with improved selectivity against other MBT-containing proteins. The antagonists described were also found to effectively interact with unlabeled endogenous L3MBTL3 in cells.
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.