ArticleJournal of virology2001
Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- Gag proteins encoded by endogenous retroviruses are required for zebrafish development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses.Science advances · 2024Article
- Identification of Cartilaginous Fish Endogenous Foamy Virus Rooting to Vertebrate Counterparts.Journal of virology · 2023Article
- Review
- The First Co-Opted Endogenous Foamy Viruses and the Evolutionary History of Reptilian Foamy Viruses.Viruses · 2019Article
- The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.Retrovirology · 2018Article
- A comparative analysis of the foamy and ortho virus capsid structures reveals an ancient domain duplication.BMC structural biology · 2017Article
- Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding.Retrovirology · 2016Article
- A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.PLoS pathogens · 2013Article
- An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity.Retrovirology · 2013Article
- The foamy virus Gag proteins: what makes them different?Viruses · 2013Review
- Genetic characterization of simian foamy viruses infecting humans.Journal of virology · 2012Article
- Article
- Review
- Basic residues in the foamy virus Gag protein.Journal of virology · 2011Article
- A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication.Retrovirology · 2011Article
- Molecular biology of foamy viruses.Medical microbiology and immunology · 2010Review
- Article
- Analysis of prototype foamy virus particle-host cell interaction with autofluorescent retroviral particles.Retrovirology · 2010Article
- Preparation of BFV Gag antiserum and preliminary study on cellular distribution of BFV.Virologica Sinica · 2010Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Retroviral Gag expression is sufficient for capsid assembly, which occurs through interaction between distinct Gag domains. Human foamy virus (HFV) capsids assemble within the cytoplasm, although their budding, which mainly occurs in the endoplasmic reticulum, requires the presence of homologous Env. Yet little is known about the molecular basis of HFV Gag precursor assembly. Using fusions between HFV Gag and a nuclear reporter protein, we have identified a strong interaction domain in the N terminus of HFV Gag which is predicted to contain a conserved coiled-coil motif. Deletion within this region in an HFV provirus abolishes viral production through inhibition of capsid assembly.
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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.