ArticleThe EMBO journal1992
Specific binding of a basic peptide from HIV-1 Rev.
Article in The EMBO journal, 1992. 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.
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
72 citing papers in PubMed, 198 citations in OpenAlex.
- Deciphering hydration patterns across RNA conformations: Insights into water-mediated RNA recognition.Current research in structural biology · 2026Article
- Mutation-driven RRE stem-loop II conformational change induces HIV-1 nuclear export dysfunction.Nucleic acids research · 2025Article
- Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev.Structure (London, England : 1993) · 2023Article
- RNA-Binding Macrocyclic Peptides.Frontiers in molecular biosciences · 2022Review
- Native mass spectrometry reveals the initial binding events of HIV-1 rev to RRE stem II RNA.Nature communications · 2020Article
- Fluorescent indicator displacement assays to identify and characterize small molecule interactions with RNA.Methods (San Diego, Calif.) · 2019Review
- Dynamic ensemble of HIV-1 RRE stem IIB reveals non-native conformations that disrupt the Rev-binding site.Nucleic acids research · 2019Article
- Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors.Nucleic acids research · 2019Article
- Molecular recognition of a branched peptide with HIV-1 Rev Response Element (RRE) RNA.Bioorganic & medicinal chemistry · 2019Article
- m6A minimally impacts the structure, dynamics, and Rev ARM binding properties of HIV-1 RRE stem IIB.PloS one · 2019Article
- Discovery of a Branched Peptide That Recognizes the Rev Response Element (RRE) RNA and Blocks HIV-1 Replication.Journal of medicinal chemistry · 2018Article
- Emerging Roles of NFrontiers in microbiology · 2018Review
- Contributions of Individual Domains to Function of the HIV-1 Rev Response Element.Journal of virology · 2017Article
- Characterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNA.Bioorganic & medicinal chemistry · 2016Article
- Effect of intercalator and Lewis acid-base branched peptide complex formation: boosting affinity towards HIV-1 RRE RNA.MedChemComm · 2016Article
- Article
- Dynamics of the human and viral m(6)A RNA methylomes during HIV-1 infection of T cells.Nature microbiology · 2016Article
- HIV-1 drug discovery: targeting folded RNA structures with branched peptides.Organic & biomolecular chemistry · 2015Article
- The HIV-1 Rev response element (RRE) adopts alternative conformations that promote different rates of virus replication.Nucleic acids research · 2015Article
- Functional analyses reveal extensive RRE plasticity in primary HIV-1 sequences selected under selective pressure.PloS one · 2014Article
12 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
4 authors at 1 institution in 1 country.
Funding
Abstract
Human immunodeficiency virus type I (HIV-1) encodes a regulatory protein, Rev, which is required for cytoplasmic expression of incompletely spliced viral mRNA. Rev activity is mediated through specific binding to a cis-acting Rev responsive element (RRE) located within the env region of HIV-1. A monomer Rev binding site corresponding to 37 nucleotides of the RRE (IIB RNA) was studied by RNA footprinting, modification interference experiments and mutational analysis. Surprisingly, a 17 amino acid peptide, corresponding to the basic domain of Rev, binds specifically to this site at essentially identical nucleotides and probably induces additional base pairing. The Rev protein and related peptide interact primarily with two sets of nucleotides located at the junction of single and double stranded regions, and at an additional site located within a helix. This suggests that the domains of proteins responsible for specific RNA binding can be remarkably small and that the interaction between RNA and protein can probably induce structure in both constituents.
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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.