ArticleProtein science : a publication of the Protein Society2025
Functional implications of hexameric dynamics in SARS-CoV-2 Nsp15.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Coronavirus Nsp15 endoribonuclease: linking viral RNA regulation to immune evasion and viral fitness.Journal of virology · 2026Review
- Article
- Functional implications of hexameric dynamics in SARS-CoV-2 Nsp15.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
19 authors.
Funding
Abstract
SARS-CoV-2, the virus responsible for the COVID-19 pandemic, has undergone continuous evolution, leading to the emergence of variants with altered transmissibility and immune evasion. For the non-structural proteins (Nsps) of SARS-CoV-2, there are limited structural analyses of their naturally occurring mutations. Here, we identified four non-synonymous single-nucleotide polymorphisms (nsSNPs) in the Epsilon lineage of SARS-CoV-2 within Nsp15, an endoribonuclease critical for immune evasion. Of these Epsilon nsSNPs, E266Q is in the catalytic domain. This study investigates the effects of this on enzymatic activity, structural stability, and oligomeric assembly by serial crystallography. By solving the structure of the Nsp15 hexamer at room temperature of both Nsp15-E266Q and WT in the P2
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