ArticleJournal of medicinal chemistry2020
Probing the Plasticity in the Active Site of Protein N-terminal Methyltransferase 1 Using Bisubstrate Analogues.
Article in Journal of medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Causal Relationship Between Serum Zinc Levels and Diabetic Kidney Disease (DKD): A Plasma Proteomics Mediation Study.Biological trace element research · 2026Article
- Mechanistic Insights into SAM-Dependent Methyltransferases: A Review of Computational Approaches.International journal of molecular sciences · 2025Review
- Structure-Guided Design of a KMT9 Inhibitor Prodrug with Cellular Activity.Journal of medicinal chemistry · 2025Article
- Structure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity.Nature communications · 2024Article
- A unique binding pocket induced by a noncanonical SAH mimic to develop potent and selective PRMT inhibitors.Acta pharmaceutica Sinica. B · 2023Article
- Cell-Effective Transition-State Analogue of PhenylethanolamineBiochemistry · 2023Article
- Structure-Activity Relationship Studies of Venglustat on NTMT1 Inhibition.Journal of medicinal chemistry · 2023Article
- Three's a crowd - why did three N-terminal methyltransferases evolve for one job?Journal of cell science · 2023Article
- Design and characterization of PROTAC degraders specific to protein N-terminal methyltransferase 1.European journal of medicinal chemistry · 2022Article
- Venglustat Inhibits Protein N-Terminal Methyltransferase 1 in a Substrate-Competitive Manner.Journal of medicinal chemistry · 2022Article
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- Analogs ofMolecular biology · 2022Article
- Discovery of a potent and dual-selective bisubstrate inhibitor for protein arginine methyltransferase 4/5.Acta pharmaceutica Sinica. B · 2021Article
- Mechanisms and inhibitors of nicotinamideRSC medicinal chemistry · 2021Review
- Past, present, and perspectives of protein N-terminal methylation.Current opinion in chemical biology · 2021Review
- Chemoproteomic Study Uncovers HemK2/KMT9 As a New Target for NTMT1 Bisubstrate Inhibitors.ACS chemical biology · 2021Article
- Structure-based Discovery of Cell-Potent Peptidomimetic Inhibitors for Protein N-Terminal Methyltransferase 1.ACS medicinal chemistry letters · 2021Article
- Structure-Based Drug Design of Bisubstrate Inhibitors of PhenylethanolamineJournal of medicinal chemistry · 2020Article
- Selective Peptidomimetic Inhibitors of NTMT1/2: Rational Design, Synthesis, Characterization, and Crystallographic Studies.Journal of medicinal chemistry · 2020Article
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7 authors.
Funding
Abstract
The bisubstrate analogue strategy is a promising approach to develop potent and selective inhibitors for protein methyltransferases. Herein, the interactions of a series of bisubstrate analogues with protein N-terminal methyltransferase 1 (NTMT1) were examined to probe the molecular properties of the active site of NTMT1. Our results indicate that a 2-C to 4-C atom linker enables its respective bisubstrate analogue to occupy both substrate- and cofactor-binding sites of NTMT1, but the bisubstrate analogue with a 5-C atom linker only interacts with the substrate-binding site and functions as a substrate. Furthermore, the 4-C atom linker is the optimal and produces the most potent inhibitor (
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