ArticleJournal of virology2002
RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 66 citations in OpenAlex.
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Characterization of viroplasm-like structures by co-expression of NSP5 and NSP2 across rotavirus species A to J.Journal of virology · 2024Article
- Iron‑sulfur clusters in viral proteins: Exploring their elusive nature, roles and new avenues for targeting infections.Biochimica et biophysica acta. Molecular cell research · 2024Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- VHS, US3 and UL13 viral tegument proteins are required for Herpes Simplex Virus-Induced modification of protein kinase R.Scientific reports · 2020Article
- Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.Journal of virology · 2020Article
- Probing the sites of interactions of rotaviral proteins involved in replication.Journal of virology · 2014Article
- The battle between rotavirus and its host for control of the interferon signaling pathway.PLoS pathogens · 2013Review
- Rotavirus non-structural proteins: structure and function.Current opinion in virology · 2012Review
- Assortment and packaging of the segmented rotavirus genome.Trends in microbiology · 2011Review
- Cyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinases.PLoS pathogens · 2010Article
- Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome.The Journal of biological chemistry · 2010Article
- Tipping the balance: antagonism of PKR kinase and ADAR1 deaminase functions by virus gene products.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2009Review
- Article
- Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2.Journal of virology · 2007Article
- Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.Journal of virology · 2006Article
- Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activities.Journal of molecular biology · 2006Article
- Hyperphosphorylation of the rotavirus NSP5 protein is independent of serine 67, [corrected] NSP2, or [corrected] the intrinsic insolubility of NSP5 is regulated by cellular phosphatases.Journal of virology · 2006Article
- Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The N- and C-terminal regions of rotavirus NSP5 are the critical determinants for the formation of viroplasm-like structures independent of NSP2.Journal of virology · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Phosphoprotein NSP5 is a component of replication intermediates that catalyze the synthesis of the segmented double-stranded RNA (dsRNA) rotavirus genome. To study the role of the protein in viral replication, His-tagged NSP5 was expressed in bacteria and purified by affinity chromatography. In vitro phosphorylation assays showed that NSP5 alone contains minimal autokinase activity but undergoes hyperphosphorylation when combined with the NTPase and helix-destabilizing protein NSP2. Hence, NSP2 mediates the hyperphosphorylation of NSP5 in the absence of other viral or cellular proteins. RNA-binding assays demonstrated that NSP5 has unique nonspecific RNA-binding activity, recognizing single-stranded RNA and dsRNA with similar affinities. The possible functions of the RNA-binding activities of NSP5 are to cooperate with NSP2 in the destabilization of RNA secondary structures and in the packaging of RNA and/or to prevent the interferon-induced dsRNA-dependent activation of the protein kinase PKR.
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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.