ArticleRNA (New York, N.Y.)2005
Arginine-rich motifs present multiple interfaces for specific binding by RNA.
Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 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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Who cites it
72 citing papers in PubMed, 126 citations in OpenAlex.
- Design and Synthesis of Odorranalectin-Derived Peptides for RNA Binding.Research square · 2026Article
- HEXIM1 inter-monomer autoinhibition governs 7SK RNA binding specificity and P-TEFb inactivation.Nature communications · 2026Article
- A conserved triple arginine motif in OMA-1 is required for RNA-binding activity and embryo viability.RNA (New York, N.Y.) · 2025Article
- The Role of Counterions in the Assembly of Charged Virus-Like Shells.The journal of physical chemistry. B · 2025Article
- Arginine: at the crossroads of nitrogen metabolism.The EMBO journal · 2025Review
- A small-molecule screen identifies novel aging modulators by targeting 5-HT/DA signaling pathway.Aging cell · 2025Article
- LCRAnnotationsDB: a database of low complexity regions functional and structural annotations.BMC genomics · 2024Article
- Beyond RNA-binding domains: determinants of protein-RNA binding.RNA (New York, N.Y.) · 2024Article
- Diversification of the Rho transcription termination factor in bacteria.Nucleic acids research · 2024Article
- The evolutionary novelty of insect defensins: from bacterial killing to toxin neutralization.Cellular and molecular life sciences : CMLS · 2024Article
- Article
- Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- LC3B is an RNA-binding protein to trigger rapid mRNA degradation during autophagy.Nature communications · 2022Article
- Z-RNA and the Flipside of the SARS Nsp13 Helicase: Is There a Role for Flipons in Coronavirus-Induced Pathology?Frontiers in immunology · 2022Article
- Role of salt-bridging interactions in recognition of viral RNA by arginine-rich peptides.Biophysical journal · 2021Article
- Lipids and Lipid Derivatives for RNA Delivery.Chemical reviews · 2021Review
- TAR RNA Mediated Folding of a Single-Arginine-Mutant HIV-1 Tat Protein within HeLa Cells Experiencing Intracellular Crowding.International journal of molecular sciences · 2021Article
- RNA origami design tools enable cotranscriptional folding of kilobase-sized nanoscaffolds.Nature chemistry · 2021Article
- The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA.Nature communications · 2021Article
- Capsid Structure ofJournal of virology · 2021Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of proteins containing arginine-rich motifs (ARMs) are known to bind RNA and are involved in regulating RNA processing in viruses and cells. Using automated selection methods we have generated a number of aptamers against ARM peptides from various natural proteins. Aptamers bind tightly to their cognate ARMs, with K(d) values in the nanomolar range, and frequently show no propensity to bind to other ARMs or even to single amino acid variants of the cognate ARM. However, at least some anti-ARM aptamers can cross-recognize a limited set of other ARMs, just as natural RNA-binding sites have been shown to exhibit so-called "chameleonism." We expand upon the number of examples of cross-recognition and, using mutational and circular dichroism (CD) analyses, demonstrate that there are multiple mechanisms by which RNA ligands can cross-recognize ARMs. These studies support a model in which individual arginine residues govern binding to an RNA ligand, and the inherent flexibility of the peptide backbone may make it possible for "semi-specific" recognition of a discrete set of RNAs by a discrete set of ARM peptides and proteins.
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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.