ArticleJournal of virology2000
Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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
46 citing papers in PubMed, 81 citations in OpenAlex.
- Review
- Article
- SLE: Novel Postulates for Therapeutic Options.Frontiers in immunology · 2020Review
- Molecular aspects of the teratogenesis of rubella virus.Biological research · 2019Review
- Article
- Rubella Viruses Shift Cellular Bioenergetics to a More Oxidative and Glycolytic Phenotype with a Strain-Specific Requirement for Glutamine.Journal of virology · 2018Article
- Altered mitochondrial dynamics as a consequence of Venezuelan Equine encephalitis virus infection.Virulence · 2017Article
- Flavivirus Infection Impairs Peroxisome Biogenesis and Early Antiviral Signaling.Journal of virology · 2015Article
- Activation of the Mitochondrial Apoptotic Signaling Platform during Rubella Virus Infection.Viruses · 2015Article
- Phosphorylation and membrane association of the Rubella virus capsid protein is important for its anti-apoptotic function.Cellular microbiology · 2014Article
- Exploration of panviral proteome: high-throughput cloning and functional implications in virus-host interactions.Theranostics · 2014Article
- Rubella virus capsid protein structure and its role in virus assembly and infection.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Activity increase in respiratory chain complexes by rubella virus with marginal induction of oxidative stress.Journal of virology · 2013Article
- Article
- Viral modulation of stress granules.Virus research · 2012Review
- Binding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifs.The Journal of general virology · 2012Article
- Rubella virus-like replicon particles: analysis of encapsidation determinants and non-structural roles of capsid protein in early post-entry replication.The Journal of general virology · 2012Article
- Analysis of subcellular G3BP redistribution during rubella virus infection.The Journal of general virology · 2012Article
- Genetic analysis in Drosophila reveals a role for the mitochondrial protein p32 in synaptic transmission.G3 (Bethesda, Md.) · 2012Article
- West Nile virus infection causes endocytosis of a specific subset of tight junction membrane proteins.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Togavirus nucleocapsids have a characteristic icosahedral structure and are composed of multiple copies of a capsid protein complexed with genomic RNA. The assembly of rubella virus nucleocapsids is unique among togaviruses in that the process occurs late in virus assembly and in association with intracellular membranes. The goal of this study was to identify host cell proteins which may be involved in regulating rubella virus nucleocapsid assembly through their interactions with the capsid protein. Capsid was used as bait to screen a CV1 cDNA library using the yeast two-hybrid system. One protein that interacted strongly with capsid was p32, a cellular protein which is known to interact with other viral proteins. The interaction between capsid and p32 was confirmed using a number of different in vitro and in vivo methods, and the site of interaction between these two proteins was shown to be at the mitochondria. Interestingly, overexpression of the rubella virus structural proteins resulted in clustering of the mitochondria in the perinuclear region. The p32-binding site in capsid is a potentially phosphorylated region that overlaps the viral RNA-binding domain of capsid. Our results are consistent with the possibility that the interaction of p32 with capsid plays a role in the regulation of nucleocapsid assembly and/or virus-host interactions.
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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.