ArticleBiochemistry2019
The Ebola Viral Protein 35 N-Terminus Is a Parallel Tetramer.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 15 citations in OpenAlex.
- 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025Review
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
- Disruption of Ebola NPJournal of molecular biology · 2023Article
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- Ebola and Marburg virus VP35 coiled-coil validated as antiviral target by tripartite split-GFP complementation.iScience · 2022Article
- Liquid Phase Partitioning in Virus Replication: Observations and Opportunities.Annual review of virology · 2022Review
- Review
- Crystal structure of human LC8 bound to a peptide from Ebola virus VP35.Journal of microbiology (Seoul, Korea) · 2021Article
- Mechanisms of Non-segmented Negative Sense RNA Viral Antagonism of Host RIG-I-Like Receptors.Journal of molecular biology · 2019Review
- Ebola virus VP35 has novel NTPase and helicase-like activities.Nucleic acids research · 2019Article
- Relevance of Ebola virus VP35 homo-dimerization on the type I interferon cascade inhibition.Antiviral chemistry & chemotherapyArticle
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Members of Mononegavirales, the order that includes nonsegmented negative sense RNA viruses (NNSVs), encode a small number of multifunctional proteins. In members of the Filoviridae family, virus protein 35 (VP35) facilitates immune evasion and functions as an obligatory cofactor for viral RNA synthesis. VP35 functions in a manner orthologous to that of phosphoproteins from other NNSVs. Although the critical roles of Ebola viral VP35 (eVP35) in immune evasion and RNA synthesis are well-appreciated, a complete understanding of its organization and its role in carrying out its many functions has yet to be fully realized. In particular, we currently lack information about the role of the oligomerization domain within eVP35. To address this limitation, we report here an investigation of the oligomer structure of eVP35 using hybrid methods that include multiangle light scattering, small-angle X-ray scattering, and cross-linking coupled with mass spectrometry to determine the shape and orientation of the eVP35 oligomer. Our integrative results are consistent with a parallel tetramer in which the N-terminal regions that are required for RNA synthesis are all oriented in the same direction. Furthermore, these results define a framework for targeting the symmetric tetramer for structure-based antiviral discovery.
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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.