ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2020
Structural Basis of Human Helicase DDX21 in RNA Binding, Unwinding, and Antiviral Signal Activation.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
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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
31 citing papers in PubMed, 44 citations in OpenAlex.
- Several multiple sequence alignment-perturbing methods enhance AlphaFold3 sampling of alternative protein states.Communications chemistry · 2026Article
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Structural and functional perspectives on DEAD-box RNA helicases in the rubber tree cold stress response.Frontiers in plant science · 2026Review
- Chemical Probe Discovery for DEAD-Box RNA-Binding Protein DDX21 Using Small-Molecule Microarrays.ACS chemical biology · 2025Article
- The DEAD-box helicase eIF4A1/2 acts as RNA chaperone during mitotic exit enabling chromatin decondensation.Nature communications · 2025Article
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- DDX21 at the Nexus of RNA Metabolism, Cancer Oncogenesis, and Host-Virus Crosstalk: Decoding Its Biomarker Potential and Therapeutic Implications.International journal of molecular sciences · 2024Review
- DExD-Box Helicase 21 Enhances Myometrial Contractions Through Thrombospondin-1-Mediated Increase in Cell Adhesion.Journal of cellular and molecular medicine · 2024Article
- U3 snoRNA inter-regulates with DDX21 in the perichromosomal region to control mitosis.Cell death & disease · 2024Article
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- Nucleolus activity-dependent recruitment and biomolecular condensation by pH sensing.Molecular cell · 2023Article
- Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.RNA (New York, N.Y.) · 2023Article
- Mechanism of 5S RNP recruitment and helicase-surveilled rRNA maturation during pre-60S biogenesis.EMBO reports · 2023Article
- Structural insights into RNase J that plays an essential role in Mycobacterium tuberculosis RNA metabolism.Nature communications · 2023Article
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- Structural analysis of the housecleaning nucleoside triphosphate pyrophosphohydrolase MazG fromFrontiers in microbiology · 2023Article
- Putting AlphaFold models to work with phenix.process_predicted_model and ISOLDE.Acta crystallographica. Section D, Structural biology · 2022Article
- Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis.Communications biology · 2022Article
- Protein purification, crystallization, and structure determination of human DEAD-box RNA helicase DDX21 in different unwinding states.STAR protocols · 2022Article
Corrections and comments
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Authors and funding
20 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA helicase DDX21 plays vital roles in ribosomal RNA biogenesis, transcription, and the regulation of host innate immunity during virus infection. How DDX21 recognizes and unwinds RNA and how DDX21 interacts with virus remain poorly understood. Here, crystal structures of human DDX21 determined in three distinct states are reported, including the apo-state, the AMPPNP plus single-stranded RNA (ssRNA) bound pre-hydrolysis state, and the ADP-bound post-hydrolysis state, revealing an open to closed conformational change upon RNA binding and unwinding. The core of the RNA unwinding machinery of DDX21 includes one wedge helix, one sensor motif V and the DEVD box, which links the binding pockets of ATP and ssRNA. The mutant D339H/E340G dramatically increases RNA binding activity. Moreover, Hill coefficient analysis reveals that DDX21 unwinds double-stranded RNA (dsRNA) in a cooperative manner. Besides, the nonstructural (NS1) protein of influenza A inhibits the ATPase and unwinding activity of DDX21 via small RNAs, which cooperatively assemble with DDX21 and NS1. The structures illustrate the dynamic process of ATP hydrolysis and RNA unwinding for RNA helicases, and the RNA modulated interaction between NS1 and DDX21 generates a fresh perspective toward the virus-host interface. It would benefit in developing therapeutics to combat the influenza virus infection.
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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.