ArticleRNA (New York, N.Y.)2005
Evolvability of the mode of peptide binding by an 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 12 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.
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
12 citing papers in PubMed, 24 citations in OpenAlex.
- Deciphering hydration patterns across RNA conformations: Insights into water-mediated RNA recognition.Current research in structural biology · 2026Article
- Structural and computational studies of HIV-1 RNA.RNA biology · 2024Review
- A Review: The Antiviral Activity of Cyclic Peptides.International journal of peptide research and therapeutics · 2023Review
- Role of salt-bridging interactions in recognition of viral RNA by arginine-rich peptides.Biophysical journal · 2021Article
- Native mass spectrometry reveals the initial binding events of HIV-1 rev to RRE stem II RNA.Nature communications · 2020Article
- Article
- Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis.Current HIV research · 2020Article
- The new (dis)order in RNA regulation.Cell communication and signaling : CCS · 2016Review
- The RNA-binding domain of bacteriophage P22 N protein is highly mutable, and a single mutation relaxes specificity toward lambda.Journal of bacteriology · 2008Article
- Non-coding RNA as a trigger of neuropathologic disorder phenotypes in transgenic Drosophila.Journal of neural transmission (Vienna, Austria : 1996) · 2008Article
- Bacteriophage P22 antitermination boxB sequence requirements are complex and overlap with those of lambda.Journal of bacteriology · 2008Article
- Specificity of phage display selected peptides for modified anticodon stem and loop domains of tRNA.The protein journal · 2007Article
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 HIV Rev-response element (RRE) RNA binds strongly to two unrelated peptides, the HIV Rev peptide and an RRE-binding aptamer, the RSG-1.2 peptide, at a similar site, but using distinct sets of interactions. In this study, the nucleotide base requirements for the binding of the RRE to the Rev and RSG-1.2 peptides were determined by selection of Rev- and RSG-1.2-binding RRE variants using a bacterial reporter system. As a result, distinct differences in the bases necessary for binding the two peptides were found in the upper stem of the RRE. Strikingly, single nucleotide changes in this region were found to switch the peptide-binding specificity of the RRE from a bifunctional Rev- and RSG-1.2-binding mode to either a Rev-specific or a RSG-1.2- specific mode, demonstrating how an RNA can evolve alternative binding strategies in discrete steps without intermediate loss of function. This evolvability of the mode of peptide binding by an RNA presumably reflects the multidimensionality of conformational space that a given RNA has available for ligand recognition, which may have been utilized in the evolution of RNA-polypeptide complexes.
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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.