ArticlemBio2017
Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.
Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Horizontal transfer of post-translational modifiers brings evolutionary opportunity and challenges to a conserved translation factor.BMC biology · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- Phosphorylation of EF-P aggravates Streptococcus suis-induced blood-brain barrier damage by enhancing serine protease production.Veterinary research · 2025Article
- Metabolic Origin, Role and Fate of the Denaturant Guanidine.Microbial biotechnology · 2025Article
- EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.Nature communications · 2024Article
- Article
- Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a potential drug targets.BBA advances · 2023Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-D-glucose epimerization in Pseudomonas putida KT2440.Scientific reports · 2021Article
- A β-hairpin epitope as novel structural requirement for protein arginine rhamnosylation.Chemical science · 2020Article
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Complex Structure ofJournal of bacteriology · 2019Article
- Switching the Post-translational Modification of Translation Elongation Factor EF-P.Frontiers in microbiology · 2019Article
- Structural basis for the glycosyltransferase activity of theThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline-specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved the crystal structure of EarP from
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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.