ArticleJournal of medicinal chemistry2011
Small-molecule ligands of methyl-lysine binding proteins.
Article in Journal of medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 119 citations in OpenAlex.
- Chemical tools targeting readers of lysine methylation.Current opinion in chemical biology · 2023Review
- Application of In Silico Filtering and Isothermal Titration Calorimetry for the Discovery of Small Molecule Inhibitors of MDM2.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Photochemical synthesis of an epigenetic focused tetrahydroquinoline library.RSC medicinal chemistry · 2021Article
- Targeting Epigenetic Mechanisms to Treat Alcohol Use Disorders (AUD).Current pharmaceutical design · 2021Article
- LEDGINs, Inhibitors of the Interaction Between HIV-1 Integrase and LEDGF/p75, Are Potent Antivirals with a Potential to Cure HIV Infection.Advances in experimental medicine and biology · 2021Article
- Targeting epigenetic protein-protein interactions with small-molecule inhibitors.Future medicinal chemistry · 2020Review
- Design and Construction of a Focused DNA-Encoded Library for Multivalent Chromatin Reader Proteins.Molecules (Basel, Switzerland) · 2020Article
- Epigenetic Control of a Local Chromatin Landscape.International journal of molecular sciences · 2020Review
- Small Molecules Targeting the Specific Domains of Histone-Mark Readers in Cancer Therapy.Molecules (Basel, Switzerland) · 2020Review
- Targeting non-bromodomain chromatin readers.Nature structural & molecular biology · 2019Review
- Targeting protein methylation: from chemical tools to precision medicines.Cellular and molecular life sciences : CMLS · 2019Review
- An Application of Fit Quality to Screen MDM2/p53 Protein-Protein Interaction Inhibitors.Molecules (Basel, Switzerland) · 2018Article
- Targeting Epigenetics in Cancer.Annual review of pharmacology and toxicology · 2018Review
- Discovery of a Highly Selective Cell-Active Inhibitor of the Histone Lysine Demethylases KDM2/7.Angewandte Chemie (International ed. in English) · 2017Article
- Chemical modulators for epigenome reader domains as emerging epigenetic therapies for cancer and inflammation.Current opinion in chemical biology · 2017Review
- Developing Spindlin1 small-molecule inhibitors by using protein microarrays.Nature chemical biology · 2017Article
- Structural basis of molecular recognition of helical histone H3 tail by PHD finger domains.The Biochemical journal · 2017Article
- Design, synthesis, and protein methyltransferase activity of a unique set of constrained amine containing compounds.Bioorganic & medicinal chemistry letters · 2016Article
- Chemical probes for methyl lysine reader domains.Current opinion in chemical biology · 2016Review
- Epigenetics: A primer for clinicians.Blood reviews · 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
16 authors at 3 institutions in 2 countries.
Funding
Abstract
Proteins which bind methylated lysines ("readers" of the histone code) are important components in the epigenetic regulation of gene expression and can also modulate other proteins that contain methyl-lysine such as p53 and Rb. Recognition of methyl-lysine marks by MBT domains leads to compaction of chromatin and a repressed transcriptional state. Antagonists of MBT domains would serve as probes to interrogate the functional role of these proteins and initiate the chemical biology of methyl-lysine readers as a target class. Small-molecule MBT antagonists were designed based on the structure of histone peptide-MBT complexes and their interaction with MBT domains determined using a chemiluminescent assay and ITC. The ligands discovered antagonize native histone peptide binding, exhibiting 5-fold stronger binding affinity to L3MBTL1 than its preferred histone peptide. The first cocrystal structure of a small molecule bound to L3MBTL1 was determined and provides new insights into binding requirements for further ligand design.
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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.