ReviewCellular and molecular life sciences : CMLS2013
RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence.
Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 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
153 citing papers in PubMed, 266 citations in OpenAlex.
- Reconstitution of antiviral Dicer activity in vitro reveals distinct contributions of RDE-4 dsRNA-binding motifs.RNA (New York, N.Y.) · 2026Article
- Structural basis for recognition of diverse localizing mRNAs by Egl-BicD.Nature structural & molecular biology · 2026Article
- Sensing of double-stranded RNA in human cells: molecular mechanisms and cellular consequences.Biochemical Society transactions · 2026Review
- Staufen dsRNA-binding domain as modules to design bifunctional antibodies for siRNA delivery.Nucleic acids research · 2026Article
- Reconstitution of antiviral Dicer activity in vitro reveals distinct contributions of RDE-4 dsRNA-binding motifs.bioRxiv : the preprint server for biology · 2025Article
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- A widespread family of viral sponge proteins reveals specific inhibition of nucleotide signals in anti-phage defense.Molecular cell · 2025Article
- Decoding RNA-Protein Interactions: Methodological Advances and Emerging Challenges.Advanced genetics (Hoboken, N.J.) · 2025Review
- Characterization of dsRNA binding proteins through solubility analysis identifies ZNF385A as a dsRNA homeostasis regulator.Nature communications · 2025Article
- PACT prevents aberrant activation of PKR by endogenous dsRNA without sequestration.Nature communications · 2025Article
- RNA binding proteins (RBPs) on genetic stability and diseases.Global medical genetics · 2025Review
- Structural basis of endo-siRNA processing by Drosophila Dicer-2 and Loqs-PD.Nucleic acids research · 2025Article
- Endo-bind-n-seq: identifying RNA motifs of RNA binding proteins isolated from endogenous sources.Life science alliance · 2025Article
- Targeting RNA-binding proteins with small molecules: perspectives and challenges.Frontiers in chemistry · 2025Review
- Effects of Molecular Crowding on the Structure, Folding, Stability, and Catalysis of RNA.Sub-cellular biochemistry · 2025Review
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- Comparative Analysis of Active LTR Retrotransposons in Sunflower (International journal of molecular sciences · 2024Article
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
- Determinants of selectivity in the dicing mechanism.Nature communications · 2024Article
- Advanced sampling simulations of coupled folding and binding of phage P22 N-peptide to boxB RNA.Biophysical journal · 2024Article
93 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The double-stranded RNA binding domain (dsRBD) is a small protein domain of 65-70 amino acids adopting an αβββα fold, whose central property is to bind to double-stranded RNA (dsRNA). This domain is present in proteins implicated in many aspects of cellular life, including antiviral response, RNA editing, RNA processing, RNA transport and, last but not least, RNA silencing. Even though proteins containing dsRBDs can bind to very specific dsRNA targets in vivo, the binding of dsRBDs to dsRNA is commonly believed to be shape-dependent rather than sequence-specific. Interestingly, recent structural information on dsRNA recognition by dsRBDs opens the possibility that this domain performs a direct readout of RNA sequence in the minor groove, allowing a global reconsideration of the principles describing dsRNA recognition by dsRBDs. We review in this article the current structural and molecular knowledge on dsRBDs, emphasizing the intricate relationship between the amino acid sequence, the structure of the domain and its RNA recognition capacity. We especially focus on the molecular determinants of dsRNA recognition and describe how sequence discrimination can be achieved by this type of domain.
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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.