ArticleJournal of molecular biology2013
Location of the dsRNA-dependent polymerase, VP1, in rotavirus particles.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 74 citations in OpenAlex.
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Single-round infectious rotaviruses with deletions of VP7 or VP4 genes, based on SA11 and WC3 strain backbones, and their potential use as viral vectors.PLoS pathogens · 2025Article
- Article
- Generation of single-round infectious rotavirus with a mutation in the intermediate capsid protein VP6.Journal of virology · 2024Article
- Sequences at gene segment termini inclusive of untranslated regions and partial open reading frames play a critical role in mammalian orthoreovirus S gene packaging.PLoS pathogens · 2024Article
- Acute rotavirus infection is associated with the induction of circulating memory CD4Scientific reports · 2023Article
- Principles of RNA recruitment to viral ribonucleoprotein condensates in a segmented dsRNA virus.eLife · 2023Article
- Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly.Communications biology · 2022Article
- Recent advances in rotavirus reverse genetics and its utilization in basic research and vaccine development.Archives of virology · 2021Review
- Review
- Capsid Structure ofJournal of virology · 2021Article
- Arrangement of the Polymerase Complexes inside a Nine-Segmented dsRNA Virus.Structure (London, England : 1993) · 2020Article
- 2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity.Science advances · 2020Article
- Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.Journal of virology · 2020Article
- Article
- In situ structures of RNA-dependent RNA polymerase inside bluetongue virus before and after uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- In situ Structure of Rotavirus VP1 RNA-Dependent RNA Polymerase.Journal of molecular biology · 2019Article
- In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.Nature communications · 2019Article
- Group A Rotavirus VP1 Polymerase and VP2 Core Shell Proteins: Intergenotypic Sequence Variation andJournal of virology · 2019Article
- Cryo-EM Reveals Architectural Diversity in Active Rotavirus Particles.Computational and structural biotechnology journal · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 6 institutions in 2 countries.
Funding
Abstract
Double-stranded RNA (dsRNA) viruses transcribe and replicate RNA within an assembled, inner capsid particle; only plus-sense mRNA emerges into the intracellular milieu. During infectious entry of a rotavirus particle, the outer layer of its three-layer structure dissociates, delivering the inner double-layered particle (DLP) into the cytosol. DLP structures determined by X-ray crystallography and electron cryomicroscopy (cryoEM) show that the RNA coils uniformly into the particle interior, avoiding a "fivefold hub" of more structured density projecting inward from the VP2 shell of the DLP along each of the twelve 5-fold axes. Analysis of the X-ray crystallographic electron density map suggested that principal contributors to the hub are the N-terminal arms of VP2, but reexamination of the cryoEM map has shown that many features come from a molecule of VP1, randomly occupying five equivalent and partly overlapping positions. We confirm here that the electron density in the X-ray map leads to the same conclusion, and we describe the functional implications of the orientation and position of the polymerase. The exit channel for the nascent transcript directs the nascent transcript toward an opening along the 5-fold axis. The template strand enters from within the particle, and the dsRNA product of the initial replication step exits in a direction tangential to the inner surface of the VP2 shell, allowing it to coil optimally within the DLP. The polymerases of reoviruses appear to have similar positions and functional orientations.
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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.