ArticleJournal of the American Chemical Society2012
Bioorthogonal profiling of protein methylation using azido derivative of S-adenosyl-L-methionine.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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.
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Who cites it
56 citing papers in PubMed, 104 citations in OpenAlex.
- Dual Stabilization ofJACS Au · 2026Article
- Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.Journal of the American Chemical Society · 2026Article
- Decoding the protein methylome: Identification, validation, and functional insights.Bioorganic & medicinal chemistry · 2025Review
- Enrichment of histone tail methylated lysine residuesChemical science · 2024Article
- Non-canonical function of histone methyltransferase G9a in the translational regulation of chronic inflammation.Cell chemical biology · 2023Article
- MePMe-seq: antibody-free simultaneous mNature communications · 2023Article
- Post-synthetic benzylation of the mRNA 5' capChemical science · 2023Article
- Functionalised Cofactor Mimics for Interactome Discovery and Beyond.Angewandte Chemie (International ed. in English) · 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
- DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2022Article
- Covalent Chemical Tools for Profiling Post-Translational Modifications.Frontiers in chemistry · 2022Review
- Characterization of SET-Domain Histone Lysine Methyltransferase Substrates Using a Cofactor S-Adenosyl-L-Methionine Surrogate.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Analogs ofMolecular biology · 2022Article
- Profiling sirtuin activity using Copper-free click chemistry.Bioorganic chemistry · 2021Article
- Profiling and Validation of Live-Cell Protein Methylation with Engineered Enzymes and Methionine Analogues.Current protocols · 2021Article
- Chemo-Enzymatic Modification of the 5' Cap Maintains Translation and Increases Immunogenic Properties of mRNA.Angewandte Chemie (International ed. in English) · 2021Article
- Enzyme-mediated bioorthogonal technologies: catalysts, chemoselective reactions and recent methyltransferase applications.Current opinion in biotechnology · 2021Review
- Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020Review
- Engineering Orthogonal Methyltransferases to Create Alternative Bioalkylation Pathways.Angewandte Chemie (International ed. in English) · 2020Article
- Methionine Adenosyltransferase Engineering to Enable Bioorthogonal Platforms for AdoMet-Utilizing Enzymes.ACS chemical biology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein methyltransferases (PMTs) play critical roles in multiple biological processes. Because PMTs often function in vivo through forming multimeric protein complexes, dissecting their activities in the native contexts is challenging but relevant. To address such a need, we envisioned a Bioorthogonal Profiling of Protein Methylation (BPPM) technology, in which a SAM analogue cofactor can be utilized by multiple rationally engineered PMTs to label substrates of the corresponding native PMTs. Here, 4-azidobut-2-enyl derivative of S-adenosyl-L-methionine (Ab-SAM) was reported as a suitable BPPM cofactor. The resultant cofactor-enzyme pairs were implemented to label specifically the substrates of closely related PMTs (e.g., EuHMT1 and EuHMT2) in a complex cellular mixture. The BPPM approach, coupled with mass spectrometric analysis, enables the identification of the nonhistone targets of EuHMT1/2. Comparison of EuHMT1/2's methylomes indicates that the two human PMTs, although similar in terms of their primary sequences, can act on the distinct sets of nonhistone targets. Given the conserved active sites of PMTs, Ab-SAM and its use in BPPM are expected to be transferable to other PMTs for target identification.
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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.