ArticlePloS one2008
The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Murine leukemia virus p12 tethers the capsid-containing pre-integration complex to chromatin by binding directly to host nucleosomes in mitosis.PLoS pathogens · 2018Article
- Distinct Particle Morphologies Revealed through Comparative Parallel Analyses of Retrovirus-Like Particles.Journal of virology · 2016Article
- Hydrodynamic and Membrane Binding Properties of Purified Rous Sarcoma Virus Gag Protein.Journal of virology · 2015Article
- The gammaretroviral p12 protein has multiple domains that function during the early stages of replication.Retrovirology · 2012Article
- Solution properties of murine leukemia virus gag protein: differences from HIV-1 gag.Journal of virology · 2011Article
- Murine leukemia viruses: objects and organisms.Advances in virology · 2011Article
- Specific insertions of zinc finger domains into Gag-Pol yield engineered retroviral vectors with selective integration properties.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag fragment that includes the N-terminal domain of CA (p12-CA(N)). Furthermore, no long range interactions were observed between the domains, as has been previously predicted. Flexibility appears to be a common feature of Gag "late" domains required for virus release during budding. Residues near the N-terminus of CA(N) that form a beta-hairpin in the mature CA protein are unfolded in p12-CA(N), consistent with proposals that hairpin formation helps trigger capsid assembly.
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Registered trials
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