ArticleNature communications2025
Regulatory role of the N-terminal intrinsically disordered region of the DEAD-box RNA helicase DDX3X in selective RNA recognition.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- An ATP-Driven N Protein-DDX21 Molecular Switch Dynamically Controls SARS-CoV-2 RNA G-Quadruplex Heterogeneity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- RNase E resolves toxic condensates by counteracting phase separation of Type II RhlB helicases.Nucleic acids research · 2026Article
- Suppression of upstream ORF translation is not a widespread mechanism of translational stimulation by yeast helicase Ded1.Nucleic acids research · 2026Article
- Microprotein Regulates G-quadruplex Driven RNA Aggregation.bioRxiv : the preprint server for biology · 2026Article
- Suppression of upstream ORF translation is not a widespread mechanism of translational stimulation by yeast helicase Ded1.bioRxiv : the preprint server for biology · 2026Article
- The human DEAD-box protein DDX3X regulates host and viral mRNA translation during Sendai Virus infection.bioRxiv : the preprint server for biology · 2026Article
- Article
- Human lncRNAProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Defining the role of RNase E in the mycobacterial degradosome-like network.bioRxiv : the preprint server for biology · 2025Article
- AlphaFlex: Ensembles of the human proteome representing disordered regions.bioRxiv : the preprint server for biology · 2025Article
- Regulatory role of the N-terminal intrinsically disordered region of the DEAD-box RNA helicase DDX3X in selective RNA recognition.Nature communications · 2025Article
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Abstract
DDX3X, a member of the DEAD-box RNA helicase family, plays a central role in the translational regulation of gene expression through its unwinding activity toward complex RNA structures in messenger RNAs (mRNAs). Although DDX3X is known to selectively stimulate the translation of a subset of genes, a specific sequence motif has not been identified; thus, the molecular mechanism underlying this selectivity remains elusive. Using solution nuclear magnetic resonance (NMR) spectroscopy, we demonstrate that the N-terminal intrinsically disordered region (IDR) of DDX3X plays a critical role in the binding and unwinding of structured RNAs. We propose that the selectivity toward target transcripts is mediated by its preferential binding to structured motifs, particularly the G-quadruplex structure, through arginine-rich segments within the N-terminal IDR. Our results provide a molecular basis for understanding translational regulation by DDX3X and highlight the remarkable role of the flexible IDR in controlling the cellular translational landscape.
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