ArticleJournal of the American Chemical Society2016
The Pseudouridine Synthases Proceed through a Glycal Intermediate.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- The impact of psuedouridine modification on human tRNA.Biochemical Society transactions · 2026Review
- Article
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- Determining the effects of pseudouridine incorporation on human tRNAs.The EMBO journal · 2025Article
- Reinvestigation of theJournal of the American Chemical Society · 2025Article
- Decoding the epitranscriptome: a new frontier for cancer therapy and drug resistance.Cell communication and signaling : CCS · 2024Review
- Decoding the 'Fifth' Nucleotide: Impact of RNA Pseudouridylation on Gene Expression and Human Disease.Molecular biotechnology · 2024Review
- Modifications in the T arm of tRNA globally determine tRNA maturation, function, and cellular fitness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Improved Sampling of Adaptive Path Collective Variables by Stabilized Extended-System Dynamics.Journal of chemical theory and computation · 2023Article
- A selective and atom-economic rearrangement of uridine by cascade biocatalysis for production of pseudouridine.Nature communications · 2023Article
- The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1.PloS one · 2023Article
- In Vitro Reconstitution of Pseudouridylation Catalyzed by Human Box H/ACA Ribonucleoprotein Particles.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure Characterization ofFrontiers in microbiology · 2022Article
- The human pseudouridine synthase PUS7 recognizes RNA with an extended multi-domain binding surface.Nucleic acids research · 2021Article
- Pseudouridines in RNAs: switching atoms means shifting paradigms.FEBS letters · 2021Review
- Structural dynamics govern substrate recruitment and catalytic turnover in H/ACA RNP pseudouridylation.RNA biology · 2021Article
- On the Track of the Missing tRNA Genes: A Source of Non-Canonical Functions?Frontiers in molecular biosciences · 2021Review
- H/ACA Small Ribonucleoproteins: Structural and Functional Comparison Between Archaea and Eukaryotes.Frontiers in microbiology · 2021Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The pseudouridine synthases isomerize (U) in RNA to pseudouridine (Ψ), and the mechanism that they follow has long been a question of interest. The recent elucidation of a product of the mechanistic probe 5-fluorouridine that had been epimerized to the arabino isomer suggested that the Ψ synthases might operate through a glycal intermediate formed by deprotonation of C2'. When that position in substrate U is deuterated, a primary kinetic isotope effect is observed, which indisputably indicates that the proposed deprotonation occurs during the isomerization of U to Ψ and establishes the mechanism followed by the Ψ synthases.
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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.