ArticleJournal of virology2012
Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of Rice black streaked dwarf 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.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- Crystal structure and nucleic acid binding mode of CPV NSP9: implications for viroplasm in Reovirales.Nucleic acids research · 2024Article
- Genetic variations and gene expression profiles of Rice Black-streaked dwarf virus (RBSDV) in different host plants and insect vectors: insights from RNA-Seq analysis.BMC genomics · 2024Article
- Structure of orthoreovirus RNA chaperone σNS, a component of viral replication factories.Nature communications · 2024Article
- Article
- A Review of Vector-Borne Rice Viruses.Viruses · 2022Review
- Development of Nanobodies against Mal de Río Cuarto virus major viroplasm protein P9-1 for diagnostic sandwich ELISA and immunodetection.Scientific reports · 2021Article
- Review on Structures of Pesticide Targets.International journal of molecular sciences · 2020Review
- Rice black-streaked dwarf virus: From multiparty interactions among plant-virus-vector to intermittent epidemics.Molecular plant pathology · 2020Article
- Rice black-streaked dwarf virus-encoded P5-1 regulates the ubiquitination activity of SCF E3 ligases and inhibits jasmonate signaling to benefit its infection in rice.The New phytologist · 2020Article
- Rice black-streaked dwarf virus P10 acts as either a synergistic or antagonistic determinant during superinfection with related or unrelated virus.Molecular plant pathology · 2019Article
- Stability of local secondary structure determines selectivity of viral RNA chaperones.Nucleic acids research · 2018Article
- Foreword to 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', a special issue in Honour of Fumio Arisaka's 70th birthday.Biophysical reviews · 2018Article
- Article
- A phloem-limited fijivirus induces the formation of neoplastic phloem tissues that house virus multiplication in the host plant.Scientific reports · 2016Article
- Article
- The molecular biology of Bluetongue virus replication.Virus research · 2014Review
- Viroplasm protein P9-1 of Rice black-streaked dwarf virus preferentially binds to single-stranded RNA in its octamer form, and the central interior structure formed by this octamer constitutes the major RNA binding site.Journal of virology · 2013Article
- Nonstructural protein P7-2 encoded by Rice black-streaked dwarf virus interacts with SKP1, a core subunit of SCF ubiquitin ligase.Virology journal · 2013Article
- New model for the genesis and maturation of viroplasms induced by fijiviruses in insect vector cells.Journal of virology · 2013Article
- Life cycle of phytoreoviruses visualized by electron microscopy and tomography.Frontiers in microbiology · 2013Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The P9-1 protein of Rice black streaked dwarf virus accumulates in viroplasm inclusions, which are structures that appear to play an important role in viral morphogenesis and are commonly found in viruses in the family Reoviridae. Crystallographic analysis of P9-1 revealed structural features that allow the protein to form dimers via hydrophobic interactions. Each dimer has carboxy-terminal regions, resembling arms, that extend to neighboring dimers, thereby uniting sets of four dimers via lateral hydrophobic interactions, to yield cylindrical octamers. The importance of these regions for the formation of viroplasm-like inclusions was confirmed by the absence of such inclusions when P9-1 was expressed without its carboxy-terminal arm. The octamers are vertically elongated cylinders resembling the structures formed by NSP2 of rotavirus, even though there are no significant similarities between the respective primary and secondary structures of the two proteins. Our results suggest that an octameric structure with an internal pore might be important for the functioning of the respective proteins in the events that occur in the viroplasm, which might include viral morphogenesis.
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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.