ArticleJournal of virology2004
Role of the C terminus of foamy virus Gag in RNA packaging and Pol expression.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 42 citations in OpenAlex.
- Intercellular Communication in the Nervous System Goes Viral.Trends in neurosciences · 2021Review
- The First Co-Opted Endogenous Foamy Viruses and the Evolutionary History of Reptilian Foamy Viruses.Viruses · 2019Article
- Review
- The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.Retrovirology · 2018Article
- Review
- Retrospective on the all-in-one retroviral nucleocapsid protein.Virus research · 2014Review
- The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation.Retrovirology · 2014Article
- Review
- The foamy virus Gag proteins: what makes them different?Viruses · 2013Review
- Foamy virus assembly with emphasis on pol encapsidation.Viruses · 2013Review
- Prototype foamy virus protease activity is essential for intraparticle reverse transcription initiation but not absolutely required for uncoating upon host cell entry.Journal of virology · 2013Article
- Expression of prototype foamy virus pol as a Gag-Pol fusion protein does not change the timing of reverse transcription.Journal of virology · 2013Article
- Foamy virus Pol protein expressed as a Gag-Pol fusion retains enzymatic activities, allowing for infectious virus production.Journal of virology · 2012Article
- Retroviral GAG proteins recruit AGO2 on viral RNAs without affecting RNA accumulation and translation.Nucleic acids research · 2012Article
- Prototype foamy virus gag nuclear localization: a novel pathway among retroviruses.Journal of virology · 2011Article
- Regulation of foamy virus protease activity by viral RNA: a novel and unique mechanism among retroviruses.Journal of virology · 2011Article
- Novel functions of prototype foamy virus Gag glycine- arginine-rich boxes in reverse transcription and particle morphogenesis.Journal of virology · 2011Article
- Foamy retrovirus integrase contains a Pol dimerization domain required for protease activation.Journal of virology · 2011Article
- A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication.Retrovirology · 2011Article
- Formation of the tRNALys packaging complex in HIV-1.FEBS letters · 2010Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Foamy viruses (FV) are complex retroviruses that possess several unique features that distinguish them from all other retroviruses. FV Gag and Pol proteins are expressed independently of one another, and both proteins undergo single cleavage events. Thus, the mature FV Gag protein does not consist of the matrix, capsid, and nucleocapsid (NC) proteins found in orthoretroviruses, and the putative NC domain of FV Gag lacks the hallmark Cys-His motifs or I domains. As there is no Gag-Pol fusion protein, the mechanism of Pol packaging is different but unknown. FV RNA packaging is not well understood either. The C terminus of FV Gag has three glycine-arginine motifs (GR boxes), the first of which has been shown to have nucleic acid binding properties in vitro. The role of these GR boxes in RNA packaging and Pol packaging was investigated with a series of Gag C-terminal truncation mutants. GR box 1 was found to be the major determinant of RNA packaging, but all three GR boxes were required to achieve wild-type levels of RNA packaging. In addition, Pol was packaged in the absence of GR box 3, but GR boxes 1 and 2 were required for efficient Pol packaging. Interestingly, the Gag truncation mutants demonstrated decreased Pol expression levels as well as defects in Pol cleavage. Thus, the C terminus of FV Gag was found to be responsible for RNA packaging, as well as being involved in the expression, cleavage, and incorporation of the Pol protein.
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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.