ArticleJournal of virology2012
Distribution and phosphorylation of the basic protein P6.9 of Autographa californica nucleopolyhedrovirus.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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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
14 citing papers in PubMed, 22 citations in OpenAlex.
- Phosphorylation of the protamine-like protein from baculovirus affects its DNA binding and virus propagation.Nucleic acids research · 2025Article
- The conserved cysteines at position 18, 36, and 49 of Autographa californica multiple nucleopolyhedrovirus VP39 are essential for virus replication.Virus genes · 2024Article
- Architecture of the baculovirus nucleocapsid revealed by cryo-EM.Nature communications · 2023Article
- Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix.Nature communications · 2021Article
- Nucleocapsid Assembly of Baculoviruses.Viruses · 2019Review
- The Autographa californica Multiple NucleopolyhedrovirusJournal of virology · 2019Article
- The 38K-Mediated Specific Dephosphorylation of the Viral Core Protein P6.9 Plays an Important Role in the Nucleocapsid Assembly of Autographa californica Multiple Nucleopolyhedrovirus.Journal of virology · 2018Article
- Protein composition analysis of polyhedra matrix of Bombyx mori nucleopolyhedrovirus (BmNPV) showed powerful capacity of polyhedra to encapsulate foreign proteins.Scientific reports · 2017Article
- Baculovirus infection induces disruption of the nuclear lamina.Scientific reports · 2017Article
- A Conserved Glycine Residue Is Required for Proper Functioning of a Baculovirus VP39 Protein.Journal of virology · 2017Article
- The Autographa californica Multiple NucleopolyhedrovirusJournal of virology · 2017Article
- The Autographa californica Multiple Nucleopolyhedrovirus ac54 Gene Is Crucial for Localization of the Major Capsid Protein VP39 at the Site of Nucleocapsid Assembly.Journal of virology · 2016Article
- Posttranslational Modifications of Baculovirus Protamine-Like Protein P6.9 and the Significance of Its Hyperphosphorylation for Viral Very Late Gene Hyperexpression.Journal of virology · 2015Article
- Autographa californica multiple nucleopolyhedrovirus orf132 encodes a nucleocapsid-associated protein required for budded-virus and multiply enveloped occlusion-derived virus production.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protamine-like protein named P6.9 is thought to play a role in the condensation of genomes of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV) during an infection. Previous studies have shown that P6.9 is phosphorylated immediately upon synthesis and dephosphorylated upon the entry of the P6.9-DNA complex into the capsid. Here, we investigate the dynamic distribution of P6.9 in AcMNPV-infected Spodoptera frugiperda cells using an influenza virus hemagglutinin (HA)-tagged P6.9. Although a portion of P6.9-HA localized to the virogenic stroma, which is the center of viral DNA replication, transcription, and nucleocapsid assembly, the majority of P6.9-HA was distributed near the inner nuclear membrane throughout the course of infection. Antiserum against P6.9 detected specific phosphorylated forms of P6.9 at the edge of, but not within, the electron-dense matte regions of the virogenic stroma. Further analysis using immunoblotting revealed that at least 11 different phosphorylated forms of P6.9, as well as dephosphorylated P6.9, were present in association with occlusion-derived virions, although only dephosphorylated P6.9 was associated with budded virions.
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