ArticleACS chemical biology2011
Expanding cofactor repertoire of protein lysine methyltransferase for substrate labeling.
Article in ACS chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 106 citations in OpenAlex.
- Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.Journal of the American Chemical Society · 2026Article
- Uncovering Enzyme-Specific Post-Translational Modifications: An Overview of Current Methods.Proteomes · 2025Review
- 18S rRNA methyltransferases DIMT1 and BUD23 drive intergenerational hormesis.Molecular cell · 2023Article
- Chemical probes and methods for the study of protein arginine methylation.RSC chemical biology · 2023Review
- Molecular probes for cellular imaging of post-translational proteoforms.RSC chemical biology · 2022Review
- Visible-Light Removable Photocaging Groups Accepted by MjMAT Variant: Structural Basis and Compatibility with DNA and RNA Methyltransferases.Chembiochem : a European journal of chemical biology · 2022Article
- Characterization of SET-Domain Histone Lysine Methyltransferase Substrates Using a Cofactor S-Adenosyl-L-Methionine Surrogate.Methods in molecular biology (Clifton, N.J.) · 2022Article
- DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2022Article
- Analogs ofMolecular biology · 2022Article
- Profiling and Validation of Live-Cell Protein Methylation with Engineered Enzymes and Methionine Analogues.Current protocols · 2021Article
- Molecular Epigenetics: Chemical Biology Tools Come of Age.Annual review of biochemistry · 2021Review
- Chemo-Enzymatic Modification of the 5' Cap Maintains Translation and Increases Immunogenic Properties of mRNA.Angewandte Chemie (International ed. in English) · 2021Article
- Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020Review
- Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases.Scientific reports · 2020Article
- Characterization of TnmH as anJournal of medicinal chemistry · 2020Article
- Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells.Molecular cell · 2020Article
- Methionine Adenosyltransferase Engineering to Enable Bioorthogonal Platforms for AdoMet-Utilizing Enzymes.ACS chemical biology · 2020Article
- Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis.Scientific reports · 2020Article
- Lysine Ethylation by Histone Lysine Methyltransferases.Chembiochem : a European journal of chemical biology · 2020Article
- Engineering Methyllysine Writers and Readers for Allele-Specific Regulation of Protein-Protein Interactions.Journal of the American Chemical Society · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein lysine methyltransferases (PKMTs) play crucial roles in normal physiology and disease processes. Profiling PKMT targets is an important but challenging task. With cancer-relevant G9a as a target, we have demonstrated success in developing S-adenosyl-L-methionine (SAM) analogues, particularly (E)-hex-2-en-5-ynyl SAM (Hey-SAM), as cofactors for engineered G9a. Hey-SAM analogue in combination with G9a Y1154A mutant modifies the same set of substrates as their native counterparts with remarkable efficiency. (E)-Hex-2-en-5-ynylated substrates undergo smooth click reaction with an azide-based probe. This approach is thus suitable for substrate characterization of G9a and expected to further serve as a starting point to evolve other PKMTs to utilize a similar set of cofactors.
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.