ReviewRNA biology2022
The Dihydrouridine landscape from tRNA to mRNA: a perspective on synthesis, structural impact and function.
Review in RNA biology, 2022. 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, 24 citations in OpenAlex.
- The mRNA covalent modification dihydrouridine regulates transcript turnover and photosynthetic capacity during plant abiotic stress.The Plant cell · 2026Article
- RNA Aptamers and Epitranscriptomics: Charting Unexplored Territories in RNA Biology.Molecular diagnosis & therapy · 2026Review
- The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.Nucleic acids research · 2026Article
- tRNA modifications in cancer: from molecular mechanisms to clinical translation.Biomarker research · 2026Review
- Structural analysis of uridine modifications in solved RNA structures.NAR genomics and bioinformatics · 2026Article
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- Quantitative CRACI reveals transcriptome-wide distribution of RNA dihydrouridine at base resolution.Nature communications · 2025Article
- Decoding the Minimal Translation System of the Plasmodium falciparum Apicoplast: Essential tRNA-modifying Enzymes and Their Roles in Organelle Maintenance.Journal of molecular biology · 2025Article
- Direct RNA sequencing of the Escherichia coli epitranscriptome uncovers alterations under heat stress.Nucleic acids research · 2025Article
- Temperature-Dependent tRNA Modifications in Bacillales.International journal of molecular sciences · 2024Article
- Exploring a unique class of flavoenzymes: Identification and biochemical characterization of ribosomal RNA dihydrouridine synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional redundancy in tRNA dihydrouridylation.Nucleic acids research · 2024Article
- Sequence- and Structure-Specific tRNA Dihydrouridylation by hDUS2.ACS central science · 2024Article
- Review
- Regulation of the epigenome through RNA modifications.Chromosoma · 2023Review
- Self-attention enabled deep learning of dihydrouridine (D) modification on mRNAs unveiled a distinct sequence signature from tRNAs.Molecular therapy. Nucleic acids · 2023Article
- Review
- The Repertoire of RNA Modifications Orchestrates a Plethora of Cellular Responses.International journal of molecular sciences · 2023Review
- Evolutionary Diversity of Dus2 Enzymes Reveals Novel Structural and Functional Features among Members of the RNA Dihydrouridine Synthases Family.Biomolecules · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The universal dihydrouridine (D) epitranscriptomic mark results from a reduction of uridine by the Dus family of NADPH-dependent reductases and is typically found within the eponym D-loop of tRNAs. Despite its apparent simplicity, D is structurally unique, with the potential to deeply affect the RNA backbone and many, if not all, RNA-connected processes. The first landscape of its occupancy within the tRNAome was reported 20 years ago. Its potential biological significance was highlighted by observations ranging from a strong bias in its ecological distribution to the predictive nature of Dus enzymes overexpression for worse cancer patient outcomes. The exquisite specificity of the Dus enzymes revealed by a structure-function analyses and accumulating clues that the D distribution may expand beyond tRNAs recently led to the development of new high-resolution mapping methods, including Rho-seq that established the presence of D within mRNAs and led to the demonstration of its critical physiological relevance.
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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.