ArticleJournal of virology2005
Analysis of human immunodeficiency virus type 1 Gag dimerization-induced assembly.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 47 citations in OpenAlex.
- Review
- Review
- How promising are HIV-1-based virus-like particles for medical applications.Frontiers in cellular and infection microbiology · 2022Review
- A Structural Perspective of the Role of IP6 in Immature and Mature Retroviral Assembly.Viruses · 2021Review
- The Functional Oligomeric State of Tegument Protein GP41 Is Essential for Baculovirus Budded Virion and Occlusion-Derived Virion Assembly.Journal of virology · 2018Article
- FRET analysis of HIV-1 Gag and GagPol interactions.FEBS open bio · 2017Article
- Comparison of Biochemical Properties of HIV-1 and HIV-2 Capsid Proteins.Frontiers in microbiology · 2017Article
- The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranes.Journal of virology · 2015Article
- Higher-order structure of the Rous sarcoma virus SP assembly domain.Journal of virology · 2014Article
- New insights into retroviral Gag-Gag and Gag-membrane interactions.Frontiers in microbiology · 2014Review
- Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.Journal of virology · 2013Article
- Wrapping up the bad news: HIV assembly and release.Retrovirology · 2013Review
- Analysis of small molecule ligands targeting the HIV-1 matrix protein-RNA binding site.The Journal of biological chemistry · 2013Article
- Antiviral activity of recombinant ankyrin targeted to the capsid domain of HIV-1 Gag polyprotein.Retrovirology · 2012Article
- Abrogation of contaminating RNA activity in HIV-1 Gag VLPs.Virology journal · 2011Article
- Determinants of the HIV-1 core assembly pathway.Virology · 2011Article
- HIV-1 matrix protein binding to RNA.Journal of molecular biology · 2011Article
- Second-site compensatory mutations of HIV-1 capsid mutations.Journal of virology · 2011Article
- Characterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assay.PloS one · 2011Article
- Multiscale computer simulation of the immature HIV-1 virion.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The nucleocapsid (NC) domains of retrovirus precursor Gag (PrGag) proteins play an essential role in virus assembly. Evidence suggests that NC binding to viral RNA promotes dimerization of PrGag capsid (CA) domains, which triggers assembly of CA N-terminal domains (NTDs) into hexamer rings that are interconnected by CA C-terminal domains. To examine the influence of dimerization on human immunodeficiency virus type 1 (HIV-1) Gag protein assembly in vitro, we analyzed the assembly properties of Gag proteins in which NC domains were replaced with cysteine residues that could be linked via chemical treatment. In accordance with the model that Gag protein pairing triggers assembly, we found that cysteine cross-linking or oxidation reagents induced the assembly of virus-like particles. However, efficient assembly also was observed to be temperature dependent or required the tethering of NTDs. Our results suggest a multistep pathway for HIV-1 Gag protein assembly. In the first step, Gag protein pairing through NC-RNA interactions or C-terminal cysteine linkage fosters dimerization. Next, a conformational change converts assembly-restricted dimers or small oligomers into assembly-competent ones. At the final stage, final particle assembly occurs, possibly through a set of larger intermediates.
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Identifiers
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.