{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ramirez-Cardenas J"],"funding":["Ministerio de Ciencia, Innovaci?n y Universidades","Departamento de Educaci?n, Cultura y Deporte, Gobierno de Arag?n","UK Research and Innovation"],"pagination":["1279-1288"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11937963"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(3)"],"pubmed_abstract":["Enteropathogenic arginine-glycosyltransferases (Arg-GTs) alter higher eukaryotic proteins by attaching a GlcNAc residue to arginine acceptor sites, disrupting essential pathways such as NF-κB signaling, which promotes bacterial survival. These enzymes are potential drug targets for treating related diseases. In this study, we present a novel STD NMR Epitope Perturbation by Mutation spectroscopic approach that, in combination with hydrogen-deuterium exchange mass spectrometry (HDX-MS), and molecular dynamics simulations, shows that the highly potent broad-spectrum anticancer drug YM155 serves as a potential noncompetitive inhibitor of these enzymes. It induces a conformation of the arginine acceptor site unfavorable for GlcNAc transfer, which underlies the molecular mechanism by which this "],"journal":["JACS Au"],"pubmed_title":["STD NMR Epitope Perturbation by Mutation Unveils the Mechanism of YM155 as an Arginine-Glycosyltransferases Inhibitor Effective in Treating Enteropathogenic Diseases."],"pmcid":["PMC11937963"],"funding_grant_id":["E34_R17","PID2022-142879NB-I00","MR/V02213X/1","LMP58_18","PID2022-136362NB-100"],"pubmed_authors":["Taleb V","Hurtado-Guerrero R","Angulo J","Zhu C","Ramirez-Cardenas J","Zhang Y","Munoz-Garcia JC","Struwe WB","Calvaresi V","Hasan K","Hardwidge PR","El Qaidi S","Veloz B"],"additional_accession":[]},"is_claimable":false,"name":"STD NMR Epitope Perturbation by Mutation Unveils the Mechanism of YM155 as an Arginine-Glycosyltransferases Inhibitor Effective in Treating Enteropathogenic Diseases.","description":"Enteropathogenic arginine-glycosyltransferases (Arg-GTs) alter higher eukaryotic proteins by attaching a GlcNAc residue to arginine acceptor sites, disrupting essential pathways such as NF-κB signaling, which promotes bacterial survival. These enzymes are potential drug targets for treating related diseases. In this study, we present a novel STD NMR Epitope Perturbation by Mutation spectroscopic approach that, in combination with hydrogen-deuterium exchange mass spectrometry (HDX-MS), and molecular dynamics simulations, shows that the highly potent broad-spectrum anticancer drug YM155 serves as a potential noncompetitive inhibitor of these enzymes. It induces a conformation of the arginine acceptor site unfavorable for GlcNAc transfer, which underlies the molecular mechanism by which this ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-02T21:12:25.557Z","creation":"2026-05-29T03:06:27.953Z"},"accession":"S-EPMC11937963","cross_references":{"pubmed":["40151243"],"doi":["10.1021/jacsau.4c01140"]}}