ArticleStructure (London, England : 1993)2023
Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser.
Article in Structure (London, England : 1993), 2023. 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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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Minimized sample consumption for time-resolved serial crystallography applied to the redox cycle of human NQO1.Communications chemistry · 2026Article
- Sample delivery methods for protein X-ray crystallography with a special focus on sample consumption.Nature communications · 2025Review
- Functional implications of hexameric dynamics in SARS-CoV-2 Nsp15.Protein science : a publication of the Protein Society · 2025Article
- Spontaneous base flipping helps drive Nsp15's preferences in double stranded RNA substrates.Nature communications · 2025Article
- Alternative substrate kinetics of SARS-CoV-2 Nsp15 endonuclease reveals a specificity landscape dominated by RNA structure.Nucleic acids research · 2024Article
- TheJournal of applied crystallography · 2024Article
- Structure-based approaches against COVID-19.Journal of the Chinese Medical Association : JCMA · 2024Review
- X-Ray Crystallography of Viruses.Sub-cellular biochemistry · 2024Review
- Review of serial femtosecond crystallography including the COVID-19 pandemic impact and future outlook.Structure (London, England : 1993) · 2023Review
- A user-friendly plug-and-play cyclic olefin copolymer-based microfluidic chip for room-temperature, fixed-target serial crystallography.Acta crystallographica. Section D, Structural biology · 2023Article
- Electrically stimulated droplet injector for reduced sample consumption in serial crystallography.Biophysical reports · 2022Article
Corrections and comments
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Authors and funding
36 authors at 6 institutions in 2 countries.
Funding
Abstract
NendoU from SARS-CoV-2 is responsible for the virus's ability to evade the innate immune system by cleaving the polyuridine leader sequence of antisense viral RNA. Here we report the room-temperature structure of NendoU, solved by serial femtosecond crystallography at an X-ray free-electron laser to 2.6 Å resolution. The room-temperature structure provides insight into the flexibility, dynamics, and other intrinsic properties of NendoU, with indications that the enzyme functions as an allosteric switch. Functional studies examining cleavage specificity in solution and in crystals support the uridine-purine cleavage preference, and we demonstrate that enzyme activity is fully maintained in crystal form. Optimizing the purification of NendoU and identifying suitable crystallization conditions set the benchmark for future time-resolved serial femtosecond crystallography studies. This could advance the design of antivirals with higher efficacy in treating coronaviral infections, since drugs that block allosteric conformational changes are less prone to drug resistance.
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