ArticleNature communications2019
In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
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Who cites it
52 citing papers in PubMed.
- In situ structure of the poxvirus portal complex.Nature · 2026Article
- Article
- A Molecular and Structural Perspective on Bluetongue Virus Entry and Assembly.Pathogens (Basel, Switzerland) · 2026Review
- Mechanism of membrane perforation in rotavirus cell entry.bioRxiv : the preprint server for biology · 2026Article
- Structure and function of the RNA polymerase complex of Borna disease virus, a nuclear-replicating non-segmented negative-strand RNA virus.Nucleic acids research · 2026Article
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Article
- Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes.Nature communications · 2024Article
- Conventional Electron Microscopy, Cryogenic Electron Microscopy, and Cryogenic Electron Tomography of Viruses.Sub-cellular biochemistry · 2024Review
- Nucleic Acid Packaging in Viruses.Sub-cellular biochemistry · 2024Review
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to CabioRxiv : the preprint server for biology · 2023Article
- Review
- Asymmetric reconstruction of the aquareovirus core at near-atomic resolution and mechanism of transcription initiation.Protein & cell · 2023Article
- A multidisciplinary approach to the identification of the protein-RNA connectome in double-stranded RNA virus capsids.Nucleic acids research · 2023Article
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- Flexibility of the Rotavirus NSP2 C-Terminal Region Supports Factory Formation via Liquid-Liquid Phase Separation.Journal of virology · 2023Article
- 14th International dsRNA Virus Symposium, Banff, Alberta, Canada, 10-14 October 2022.Virus research · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Transcribing and replicating a double-stranded genome require protein modules to unwind, transcribe/replicate nucleic acid substrates, and release products. Here we present in situ cryo-electron microscopy structures of rotavirus dsRNA-dependent RNA polymerase (RdRp) in two states pertaining to transcription. In addition to the previously discovered universal "hand-shaped" polymerase core domain shared by DNA polymerases and telomerases, our results show the function of N- and C-terminal domains of RdRp: the former opens the genome duplex to isolate the template strand; the latter splits the emerging template-transcript hybrid, guides genome reannealing to form a transcription bubble, and opens a capsid shell protein (CSP) to release the transcript. These two "helicase" domains also extensively interact with CSP, which has a switchable N-terminal helix that, like cellular transcriptional factors, either inhibits or promotes RdRp activity. The in situ structures of RdRp, CSP, and RNA in action inform mechanisms of not only transcription, but also replication.
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Registered trials
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