ArticleJournal of virology2017
Contributions of Individual Domains to Function of the HIV-1 Rev Response Element.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Mutation-driven RRE stem-loop II conformational change induces HIV-1 nuclear export dysfunction.Nucleic acids research · 2025Article
- Structure of HIV-1 RRE stem-loop II identifies two conformational states of the high-affinity Rev binding site.Nature communications · 2024Article
- Creation of the HIV-1 antisense geneMicrobiology spectrum · 2024Article
- HIVIntact: a python-based tool for HIV-1 genome intactness inference.Retrovirology · 2021Article
- Structural Mimicry Drives HIV-1 Rev-Mediated HERV-K Expression.Journal of molecular biology · 2020Article
- HIV Rev-isited.Open biology · 2020Review
- Sequence and Functional Variation in the HIV-1 Rev Regulatory Axis.Current HIV research · 2020Article
- Combined HIV-1 sequence and integration site analysis informs viral dynamics and allows reconstruction of replicating viral ancestors.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Highly Mutable Linker Regions Regulate HIV-1 Rev Function and Stability.Scientific reports · 2019Article
- A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export.Journal of structural biology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The HIV-1 Rev response element (RRE) is a 351-base element in unspliced and partially spliced viral RNA; binding of the RRE by the viral Rev protein induces nuclear export of RRE-containing RNAs, as required for virus replication. It contains one long, imperfect double helix (domain I), one branched domain (domain II) containing a high-affinity Rev-binding site, and two or three additional domains. We previously reported that the RRE assumes an "A" shape in solution and suggested that the location of the Rev binding sites in domains I and II, opposite each other on the two legs of the A, is optimal for Rev binding and explains Rev's specificity for RRE-containing RNAs. Using small-angle X-ray scattering (SAXS) and a quantitative functional assay, we have now analyzed a panel of RRE mutants. All the results support the essential role of the A shape for RRE function. Moreover, they suggest that the distal portion of domain I and the three crowning domains all contribute to the maintenance of the A shape. Domains I and II are necessary and sufficient for substantial RRE function, provided they are joined by a flexible linker that allows the two domains to face each other.
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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.