ArticleJournal of virology2012
Cryo-electron tomography of rubella virus.
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 21 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
21 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Rubella Virus Infections: A Bibliometric Analysis of the Scientific Literature from 2000 to 2021.Healthcare (Basel, Switzerland) · 2022Article
- Article
- Exogenous Rubella Virus Capsid Proteins Enhance Virus Genome Replication.Pathogens (Basel, Switzerland) · 2022Article
- Molecular and Structural Insights into the Life Cycle of Rubella Virus.Journal of virology · 2021Review
- T Lymphocytes as Measurable Targets of Protection and Vaccination Against Viral Disorders.International review of cell and molecular biology · 2019Review
- Molecular Requirements for Self-Interaction of the Respiratory Syncytial Virus Matrix Protein in Living Mammalian Cells.Viruses · 2018Article
- Analysis of VSV pseudotype virus infection mediated by rubella virus envelope proteins.Scientific reports · 2017Article
- Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.PLoS pathogens · 2017Article
- The Density Code for the Development of a Vaccine?Journal of pharmaceutical sciences · 2016Review
- Calcium-Dependent Rubella Virus Fusion Occurs in Early Endosomes.Journal of virology · 2016Article
- Morphology and Molecular Composition of Purified Bovine Viral Diarrhea Virus Envelope.PLoS pathogens · 2016Article
- Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion.Viruses · 2016Review
- Application of Oral Fluid Assays in Support of Mumps, Rubella and Varicella Control Programs.Vaccines · 2015Review
- Rubella.Lancet (London, England) · 2015Review
- Viral membrane fusion.Virology · 2015Review
- BST2/tetherin inhibition of alphavirus exit.Viruses · 2015Article
- Rubella virus: first calcium-requiring viral fusion protein.PLoS pathogens · 2014Article
- Relating structure to evolution in class II viral membrane fusion proteins.Current opinion in virology · 2014Review
- 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
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Rubella virus is the only member of the Rubivirus genus within the Togaviridae family and is the causative agent of the childhood disease known as rubella or German measles. Here, we report the use of cryo-electron tomography to examine the three-dimensional structure of rubella virions and compare their structure to that of Ross River virus, a togavirus belonging the genus Alphavirus. The ectodomains of the rubella virus glycoproteins, E1 and E2, are shown to be organized into extended rows of density, separated by 9 nm on the viral surface. We also show that the rubella virus nucleocapsid structure often forms a roughly spherical shell which lacks high density at its center. While many rubella virions are approximately spherical and have dimensions similar to that of the icosahedral Ross River virus, the present results indicate that rubella exhibits a large degree of pleomorphy. In addition, we used rotation function calculations and other analyses to show that approximately spherical rubella virions lack the icosahedral organization which characterizes Ross River and other alphaviruses. The present results indicate that the assembly mechanism of rubella virus, which has previously been shown to differ from that of the alphavirus assembly pathway, leads to an organization of the rubella virus structural proteins that is different from that of alphaviruses.
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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.