ArticleACS omega2025
Substrate Specificities of DDX1: A Human DEAD-Box Protein.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Selective Reprogramming of Ribosome Assembly and Translational Control during Bacterial Growth Phase Transitions.ACS omega · 2026Article
- ACOD1 deficiency promotes DDX1 methylation-mediated mitochondrial dysfunction and dermal papilla cell senescence in androgenetic alopecia.BMC medicine · 2026Article
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- Targeting R-loops: diverse RNA helicases in R-loop resolution and their potential as targets for cancer therapy.Frontiers in cell and developmental biology · 2026Review
- Optimization of a malachite green-pyrophosphatase assay for the Zika virus RNA-dependent RNA polymerase and preliminary identification of natural product modulators.Frontiers in drug discovery · 2026Article
- Discovery of Inhibitors Targeting the RNA-Dependent RNA Polymerase of the Zika Virus.bioRxiv : the preprint server for biology · 2025Article
- DDX1 methylation mediated MATR3 splicing regulates intervertebral disc degeneration by initiating chromatin reprogramming.Nature communications · 2025Article
- Phase-Specific Antibiotic Resistance Mechanisms in anbioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
DDX1 is a human DEAD-box RNA helicase involved in various stages of RNA metabolism, from transcription to decay, and is consequently implicated in many human diseases. The nucleotides hydrolyzed by DDX1 and the structures of the nucleic acids upon which it acts in cells remain largely unknown. In this study, we identify the nucleic acid sequences and structures that support DDX1's nucleotide hydrolysis activity and determine its nucleotide hydrolysis specificity. Our data demonstrate that DDX1 hydrolyzes only ATP and deoxy-ATP in the presence of RNA. The ATP hydrolysis activity of DDX1 is stimulated by single-stranded RNA molecules as short as ten nucleotides, a blunt-ended double-stranded RNA, double-stranded RNA/DNA hybrid, and single-stranded DNA. Under our experimental conditions, single-stranded DNA stimulates DDX1's ATPase activity to a smaller extent compared to the other RNA constructs or the RNA/DNA hybrid. Given DDX1's involvement in numerous critical cellular processes and its implication in various human diseases, determining its substrate specificity not only enhances our understanding of its
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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.