ArticleBioorganic & medicinal chemistry2016
Characterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNA.
Article in Bioorganic & medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 16 citations in OpenAlex.
- The Boron Advantage: The Evolution and Diversification of Boron's Applications in Medicinal Chemistry.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Limited nucleotide changes of HIV-1 subtype B Rev response element in China affect overall Rev-RRE activity and viral replication.Frontiers in microbiology · 2022Article
- Merging the Versatile Functionalities of Boronic Acid with Peptides.International journal of molecular sciences · 2021Review
- Boronic Acids and Their Derivatives in Medicinal Chemistry: Synthesis and Biological Applications.Molecules (Basel, Switzerland) · 2020Review
- Discovery of a Branched Peptide That Recognizes the Rev Response Element (RRE) RNA and Blocks HIV-1 Replication.Journal of medicinal chemistry · 2018Article
- Branched Peptides: Acridine and Boronic Acid Derivatives as Antimicrobial Agents.ACS medicinal chemistry letters · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
A branched peptide containing multiple boronic acids was found to bind RRE IIB selectively and inhibit HIV-1 p24 capsid production in a dose-dependent manner. Structure-activity relationship studies revealed that branching in the peptide is crucial for the low micromolar binding towards RRE IIB, and the peptide demonstrates selectivity towards RRE IIB in the presence of tRNA. Footprinting studies suggest a binding site on the upper stem and internal loop regions of the RNA, which induces enzymatic cleavage of the internal loops of RRE IIB upon binding.
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Identifiers
What OpenQuestion holds
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.