ArticleArchives of virology2011
Investigations on the RNA binding and phosphorylation of groundnut bud necrosis virus nucleocapsid protein.
Article in Archives of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 11 citations in OpenAlex.
- Groundnut bud necrosis orthotospovirus: An emerging viral problem of pulse crops.Archives of virology · 2026Review
- Five questions on the cell-to-cell movement ofBBA advances · 2024Article
- Raman-dielectrophoresis goes viral: towards a rapid and label-free platform for plant virus characterization.Frontiers in microbiology · 2023Article
- Phosphorylation regulates the subcellular localization of Cucumber Mosaic Virus 2b protein.Scientific reports · 2017Article
- Phosphorylation of Beet black scorch virus coat protein by PKA is required for assembly and stability of virus particles.Scientific reports · 2015Article
- Two key arginine residues in the coat protein of Bamboo mosaic virus differentially affect the accumulation of viral genomic and subgenomic RNAs.Molecular plant pathology · 2014Article
- Groundnut bud necrosis virus encoded NSm associates with membranes via its C-terminal domain.PloS one · 2014Article
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
Groundnut bud necrosis virus belongs to the genus Tospovirus, infects a wide range of crop plants and causes severe losses. To understand the role of the nucleocapsid protein in the viral life cycle, the protein was overexpressed in E. coli and purified by Ni-NTA chromatography. The purified N protein was well folded and was predominantly alpha-helical. Deletion analysis revealed that the C-terminal unfolded region of the N protein was involved in RNA binding. Furthermore, the N protein could be phosphorylated in vitro by Nicotiana benthamiana plant sap and by purified recombinant kinases such as protein kinase CK2 and calcium-dependent protein kinase. This is the first report of phoshphorylation of a nucleocapsid protein in the family Bunyaviridae. The possible implications of the present findings for the viral life cycle are discussed.
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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.