ArticleJournal of virology2006
Human immunodeficiency virus type 1 Gag polyprotein modulates its own translation.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed, 65 citations in OpenAlex.
- Upstream of N-Ras (Unr/CSDE1) Interacts with NCp7 and Gag, Modulating HIV-1 IRES-Mediated Translation Initiation.Viruses · 2022Article
- A novel role for gag as a cis-acting element regulating RNA structure, dimerization and packaging in HIV-1 lentiviral vectors.Nucleic acids research · 2022Article
- When liquid-liquid phase separation meets viral infections.Frontiers in immunology · 2022Review
- HIV-1 Packaging Visualised by In-Gel SHAPE.Viruses · 2021Article
- Potential Achilles heels of SARS-CoV-2 are best displayed by the base order-dependent component of RNA folding energy.Computational biology and chemistry · 2021Article
- Visualizing the translation and packaging of HIV-1 full-length RNA.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Focus on Translation Initiation of the HIV-1 mRNAs.International journal of molecular sciences · 2018Review
- Reovirus Nonstructural Protein σNS Acts as an RNA Stability Factor Promoting Viral Genome Replication.Journal of virology · 2018Article
- Identifying the assembly intermediate in which Gag first associates with unspliced HIV-1 RNA suggests a novel model for HIV-1 RNA packaging.PLoS pathogens · 2018Article
- The basal translation rate of authentic HIV-1 RNA is regulated by 5'UTR nt-pairings at junction of R and U5.Scientific reports · 2017Article
- Subcellular Localization of HIV-1Journal of virology · 2017Article
- Orchestrating the Selection and Packaging of Genomic RNA by Retroviruses: An Ensemble of Viral and Host Factors.Viruses · 2016Review
- Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling.Retrovirology · 2016Article
- Review
- Structural domains within the HIV-1 mRNA and the ribosomal protein S25 influence cap-independent translation initiation.The FEBS journal · 2016Article
- Translational Control of the HIV Unspliced Genomic RNA.Viruses · 2015Review
- HIV-2 genomic RNA accumulates in stress granules in the absence of active translation.Nucleic acids research · 2014Article
- Translation initiation of the HIV-1 mRNA.Translation (Austin, Tex.) · 2014Review
- Article
- An HIV-1 replication pathway utilizing reverse transcription products that fail to integrate.Journal of virology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The full-length viral RNA of human immunodeficiency virus type 1 (HIV-1) functions both as the mRNA for the viral structural proteins Gag and Gag/Pol and as the genomic RNA packaged within viral particles. The packaging signal which Gag recognizes to initiate genome encapsidation is in the 5' untranslated region (UTR) of the HIV-1 RNA, which is also the location of translation initiation complex formation. Hence, it is likely that there is competition between the translation and packaging processes. We studied the ability of Gag to regulate translation of its own mRNA. Gag had a bimodal effect on translation from the HIV-1 5' UTR, stimulating translation at low concentrations and inhibiting translation at high concentrations in vitro and in vivo. The inhibition was dependent upon the ability of Gag to bind the packaging signal through its nucleocapsid domain. The stimulatory activity was shown to depend on the matrix domain of Gag. These results suggest that Gag controls the equilibrium between translation and packaging, ensuring production of enough molecules of Gag to make viral particles before encapsidating its genome.
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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.