ArticleJournal of virology2002
Molecular organization of Mason-Pfizer monkey virus capsids assembled from Gag polyprotein in Escherichia coli.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity.Retrovirology · 2014Article
- Higher-order structure of the Rous sarcoma virus SP assembly domain.Journal of virology · 2014Article
- Effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and human immunodeficiency virus.Journal of virology · 2010Article
- The impact of altered polyprotein ratios on the assembly and infectivity of Mason-Pfizer monkey virus.Virology · 2009Article
- The structural biology of HIV assembly.Current opinion in structural biology · 2008Review
- Multimerization of the p12 domain is necessary for Mason-Pfizer monkey virus Gag assembly in vitro.Virology · 2007Article
- Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.Journal of virology · 2006Article
- Distinct roles for nucleic acid in in vitro assembly of purified Mason-Pfizer monkey virus CANC proteins.Journal of virology · 2006Article
- Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging.Protein science : a publication of the Protein Society · 2005Article
- Functional surfaces of the human immunodeficiency virus type 1 capsid protein.Journal of virology · 2003Article
- Structural organization of authentic, mature HIV-1 virions and cores.The EMBO journal · 2003Article
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Authors and funding
6 authors at 6 institutions in 4 countries.
Funding
Abstract
We describe the results of a study by electron microscopy and image processing of Gag protein shells-immature capsids--of Mason-Pfizer monkey virus assembled in Escherichia coli from two truncated forms of the Gag precursor: Deltap4Gag, in which the C-terminal p4Gag was deleted, and Pro(-)CA.NC, in which the N-terminal peptides and proline 1 of the CA domain were deleted. Negative staining of capsids revealed small patches of holes forming a trigonal or hexagonal pattern most clearly visible on occasional tubular forms. The center-to-center spacing of holes in the network was 7.1 nm in Deltap4Gag capsids and 7.4 nm in Pro(-)CA.NC capsids. Image processing of Deltap4Gag tubes revealed a hexagonal network of holes formed by six subunits with a single subunit shared between rings. This organization suggests that the six subunits are contributed by three trimers of the truncated Gag precursor. Similar molecular organization was observed in negatively stained Pro(-)CA.NC capsids. Shadowed replicas of freeze-etched capsids produced by either construct confirmed the presence of a hexagonal network of holes with a similar center-to-center spacing. We conclude that the basic building block of the cage-like network is a trimer of the Deltap4Gag or Pro(-)CA.NC domains. In addition, our results point to a key role of structurally constrained CA domain in the trimeric interaction of the Gag polyprotein.
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