ArticleJournal of molecular biology2017
Biochemical Differences and Similarities between the DEAD-Box Helicase Orthologs DDX3X and Ded1p.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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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.
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Who cites it
42 citing papers in PubMed, 59 citations in OpenAlex.
- Review
- DDX3X Syndrome: Clinical, Neuroimaging, AI-Assisted Facial Profiling and Genotype-Phenotype Correlations.Genes · 2026Observational
- DDX3X acts as a selective dual switch regulator of mRNA translation in acute ER stress.Cell reports · 2025Article
- Unraveling the mechanism of RNA duplex unwinding by DEAD-box helicase DDX3X: Insights into Cooperativity and roles of protomers.Biochemical and biophysical research communications · 2025Article
- Regulatory role of the N-terminal intrinsically disordered region of the DEAD-box RNA helicase DDX3X in selective RNA recognition.Nature communications · 2025Article
- DEAD-box helicase intrinsically disordered domains and structural dynamics of HIV-1 RNA are required to reveal DDX3X catalytic efficiency.Nucleic acids research · 2025Article
- Substrate Specificities of DDX1: A Human DEAD-Box Protein.ACS omega · 2025Article
- Post-transcriptional cross- and auto-regulation buffer expression of the human RNA helicasesGenome research · 2025Article
- Multi-modal investigation reveals pathogenic features of diverse DDX3X missense mutations.PLoS genetics · 2025Article
- RNA helicases DDX3X and DDX3Y form nanometer-scale RNA-protein clusters that support catalytic activity.Current biology : CB · 2024Article
- The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024Review
- Specific catalytically impaired DDX3X mutants form sexually dimorphic hollow condensates.Nature communications · 2024Article
- Post-transcriptional cross- and auto-regulation buffer expression of the human RNA helicasesbioRxiv : the preprint server for biology · 2024Article
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- Review
- RNA helicase DDX3 regulates RAD51 localization and DNA damage repair in Ewing sarcoma.iScience · 2024Article
- Substrate Specificities of DDX1: A Human DEAD-box protein.bioRxiv : the preprint server for biology · 2024Article
- Regulation and mechanisms of action of RNA helicases.RNA biology · 2024Review
- Liquid-liquid phase separation in DNA double-strand breaks repair.Cell death & disease · 2023Review
- The Viral Protein K7 Inhibits Biochemical Activities and Condensate Formation by the DEAD-box Helicase DDX3X.Journal of molecular biology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DDX3X is a conserved DEAD-box RNA helicase involved in translation initiation and other processes of RNA metabolism. Mutations in human DDX3X and deregulation of its expression are linked to tumorigenesis and intellectual disability. The protein is also targeted by diverse viruses. Previous studies demonstrated helicase and NTPase activities for DDX3X, but important biochemical features of the enzyme remain unclear. Here, we systematically characterize enzymatic activities of human DDX3X and compare these to its closely related Saccharomyces cerevisiae ortholog Ded1p. We show that DDX3X, like Ded1p, utilizes exclusively adenosine triphosphates to unwind helices, oligomerizes to function as efficient RNA helicase, and does not unwind DNA duplexes. The ATPase activity of DDX3X is markedly stimulated by RNA and weaker by DNA, although DNA binds to the enzyme. For RNA unwinding, DDX3X shows a greater preference than Ded1p for substrates with unpaired regions 3' to the duplex over those with 5' unpaired regions. DDX3X separates longer RNA duplexes faster than Ded1p and is less potent than Ded1p in facilitating strand annealing. Our results reveal that the biochemical activities of human DDX3X are typical for DEAD-box RNA helicases, but diverge quantitatively from its highly similar S. cerevisiae ortholog Ded1p.
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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.