ArticleJournal of virology2021
Structural Analysis of the OC43 Coronavirus 2'-O-RNA Methyltransferase.
Article in Journal of virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Current Status and Challenges of Vaccine Development for Seasonal Human Coronaviruses.Vaccines · 2025Review
- Structural insights into the assembly and regulation of 2'-O RNA methylation by SARS-CoV-2 nsp16/nsp10.Structure (London, England : 1993) · 2025Article
- Structure of SARS-CoV-2 MTase nsp14 with the inhibitor STM957 reveals inhibition mechanism that is shared with a poxviral MTase VP39.Journal of structural biology: X · 2024Article
- Discovery and structural characterization of monkeypox virus methyltransferase VP39 inhibitors reveal similarities to SARS-CoV-2 nsp14 methyltransferase.Nature communications · 2023Article
- SS148 and WZ16 inhibit the activities of nsp10-nsp16 complexes from all seven human pathogenic coronaviruses.Biochimica et biophysica acta. General subjects · 2023Article
- Crystal structure of SARS-CoV-2 nsp10-nsp16 in complex with small molecule inhibitors, SS148 and WZ16.Protein science : a publication of the Protein Society · 2022Article
- Coronaviral RNA-methyltransferases: function, structure and inhibition.Nucleic acids research · 2022Article
- Applying polypharmacology approach for drug repurposing for SARS-CoV2.Journal of chemical sciences (Bangalore, India) · 2022Article
- Article
- Localization of SARS-CoV-2 Capping Enzymes Revealed by an Antibody against the nsp10 Subunit.Viruses · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The OC43 coronavirus is a human pathogen that usually causes only the common cold. One of its key enzymes, similar to other coronaviruses, is the 2'-O-RNA methyltransferase (MTase), which is essential for viral RNA stability and expression. Here, we report the crystal structure of the 2'-O-RNA MTase in a complex with the pan-methyltransferase inhibitor sinefungin solved at 2.2-Å resolution. The structure reveals an overall fold consistent with the fold observed in other coronaviral MTases. The major differences are in the conformation of the C terminus of the nsp16 subunit and an additional helix in the N terminus of the nsp10 subunits. The structural analysis also revealed very high conservation of the
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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.