ArticleProceedings of the National Academy of Sciences of the United States of America2010
Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 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
83 citing papers in PubMed, 128 citations in OpenAlex.
- Structural basis for HIV-1 Rev recognition by the histone chaperone human Nap1.The Journal of biological chemistry · 2026Article
- The HIV-1 nuclear export complex reveals the role of RNA in CRM1 cargo recognition.Molecular cell · 2025Article
- Article
- Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev.Structure (London, England : 1993) · 2023Article
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- Tuning Rex rules HTLV-1 pathogenesis.Frontiers in immunology · 2022Review
- Role of salt-bridging interactions in recognition of viral RNA by arginine-rich peptides.Biophysical journal · 2021Article
- Identification of host proteins differentially associated with HIV-1 RNA splice variants.eLife · 2021Article
- Review
- Structural Mimicry Drives HIV-1 Rev-Mediated HERV-K Expression.Journal of molecular biology · 2020Article
- HIV-1 resists MxB inhibition of viral Rev protein.Emerging microbes & infections · 2020Article
- HIV Rev-isited.Open biology · 2020Review
- Structural basis of prostate-specific membrane antigen recognition by the A9g RNA aptamer.Nucleic acids research · 2020Article
- Emergence and molecular mechanisms of SARS-CoV-2 and HIV to target host cells and potential therapeutics.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2020Review
- Nucleic acid recognition and antiviral activity of 1,4-substituted terphenyl compounds mimicking all faces of the HIV-1 Rev protein positively-charged α-helix.Scientific reports · 2020Article
- Review
- Exploring the RNA-Recognition Mechanism Using Supervised Molecular Dynamics (SuMD) Simulations: Toward a Rational Design for Ribonucleic-Targeting Molecules?Frontiers in chemistry · 2020Article
- Evolution of the HIV-1 Rev Response Element during Natural Infection Reveals Nucleotide Changes That Correlate with Altered Structure and Increased Activity over Time.Journal of virology · 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
- Highly Mutable Linker Regions Regulate HIV-1 Rev Function and Stability.Scientific reports · 2019Article
23 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
8 authors at 5 institutions in 2 countries.
Funding
Abstract
HIV-1 Rev is a small regulatory protein that mediates the nuclear export of viral mRNAs, an essential step in the HIV replication cycle. In this process Rev oligomerizes in association with a highly structured RNA motif, the Rev response element. Crystallographic studies of Rev have been hampered by the protein's tendency to aggregate, but Rev has now been found to form a stable soluble equimolar complex with a specifically engineered monoclonal Fab fragment. We have determined the structure of this complex at 3.2 A resolution. It reveals a molecular dimer of Rev, bound on either side by a Fab, where the ordered portion of each Rev monomer (residues 9-65) contains two coplanar alpha-helices arranged in hairpin fashion. Subunits dimerize through overlapping of the hairpin prongs. Mating of hydrophobic patches on the outer surface of the dimer is likely to promote higher order interactions, suggesting a model for Rev oligomerization onto the viral RNA.
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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.