ArticleJournal of virology2005
In vivo self-interaction of nodavirus RNA replicase protein a revealed by fluorescence resonance energy transfer.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
30 citing papers in PubMed, 49 citations in OpenAlex.
- Evolution of RNA Viruses: Reasons for the Existence of Separate Plus, Minus, and Double-Strand Replication Strategies.Viruses · 2024Article
- Multifunctional Protein A Is the Only Viral Protein Required for Nodavirus RNA Replication Crown Formation.Viruses · 2022Article
- Cryo-electron microscopy of nodavirus RNA replication organelles illuminates positive-strand RNA virus genome replication.Current opinion in virology · 2021Review
- Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Role of Mitochondrial Membrane Spherules in Flock House Virus Replication.Journal of virology · 2016Article
- Review
- Sequence analysis reveals a conserved extension in the capping enzyme of the alphavirus supergroup, and a homologous domain in nodaviruses.Biology direct · 2015Article
- Rapid evolution of virus sequences in intrinsically disordered protein regions.PLoS pathogens · 2014Article
- The RNA binding of protein A from Wuhan nodavirus is mediated by mitochondrial membrane lipids.Virology · 2014Article
- Flock house virus RNA polymerase initiates RNA synthesis de novo and possesses a terminal nucleotidyl transferase activity.PloS one · 2014Article
- Article
- The self-interaction of a nodavirus replicase is enhanced by mitochondrial membrane lipids.PloS one · 2014Article
- Characterization of a nodavirus replicase revealed a de novo initiation mechanism of RNA synthesis and terminal nucleotidyltransferase activity.The Journal of biological chemistry · 2013Article
- Architecture and biogenesis of plus-strand RNA virus replication factories.World journal of virology · 2013Review
- Virus factories: biogenesis and structural design.Cellular microbiology · 2013Review
- Bromovirus RNA replication compartment formation requires concerted action of 1a's self-interacting RNA capping and helicase domains.Journal of virology · 2012Article
- Interstitial contacts in an RNA-dependent RNA polymerase lattice.Journal of molecular biology · 2011Article
- NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes.Journal of virology · 2011Article
- Viral infection: Moving through complex and dynamic cell-membrane structures.Communicative & integrative biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Flock house virus (FHV) is the best-characterized member of the Nodaviridae, a family of small, positive-strand RNA viruses. Unlike most RNA viruses, FHV encodes only a single polypeptide, protein A, that is required for RNA replication. Protein A contains a C-proximal RNA-dependent RNA polymerase domain and localizes via an N-terminal transmembrane domain to the outer mitochondrial membrane, where FHV RNA replication takes place in association with invaginations referred to as spherules. We demonstrate here that protein A self-interacts in vivo by using flow cytometric analysis of fluorescence resonance energy transfer (FRET), spectrofluorometric analysis of bioluminescence resonance energy transfer, and coimmunoprecipitation. Several nonoverlapping protein A sequences were able to independently direct protein-protein interaction, including an N-terminal region previously shown to be sufficient for localization to the outer mitochondrial membrane (D. J. Miller and P. Ahlquist, J. Virol. 76:9856-9867, 2000). Mutations in protein A that diminished FRET also diminished FHV RNA replication, a finding consistent with an important role for protein A self-interaction in FHV RNA synthesis. Thus, the results imply that FHV protein A functions as a multimer rather than as a monomer at one or more steps in RNA replication.
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What OpenQuestion holds
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.