ArticleBiomolecular NMR assignments2017
Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus.
Article in Biomolecular NMR assignments, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Structural characterization of a soil viral auxiliary metabolic gene product - a functional chitosanase.Nature communications · 2022Article
- Human Tibroviruses: Commensals or Lethal Pathogens?Viruses · 2020Review
- Human, Nonhuman Primate, and Bat Cells Are Broadly Susceptible to Tibrovirus Particle Cell Entry.Frontiers in microbiology · 2019Article
- Solution NMR structures of oxidized and reduced Ehrlichia chaffeensis thioredoxin: NMR-invisible structure owing to backbone dynamics.Acta crystallographica. Section F, Structural biology communications · 2018Article
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Abstract
The Bas-Congo virus (BASV) is the first rhabdovirus associated with a human outbreak of acute hemorrhagic fever. The single-stranded, negative-sense RNA genome of BASV contains the five core genes present in all rhabdoviral genomes plus an additional three genes, annotated U1, U2, and U3, with weak (<21%) sequence similarity only to a handful of genes observed in a few other rhabdoviral genomes. The function of the rhabdoviral U proteins is unknown, but, they are hypothesized to play a role in viral infection or replication. To better understand this unique family of proteins, a construct containing residues 27-203 of the 216-residue U1 protein (BASV-U1*) was prepared. By collecting data in 0.5 M urea it was possible to eliminate transient association enough to enable the assignment of most of the observable
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