ArticleJournal of virology2013
Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 87 citations in OpenAlex.
- Article
- Unveiling the structural and functional implications of uncharacterized NSPs and variations in the molecular toolkit across arteriviruses.NAR genomics and bioinformatics · 2025Article
- Natural evidence of coronaviral 2'-O-methyltransferase activity affecting viral pathogenesis via improved substrate RNA binding.Signal transduction and targeted therapy · 2024Article
- Multiple Lines of Evidence Support 199 SARS-CoV-2 Positively Selected Amino Acid Sites.International journal of molecular sciences · 2024Article
- SARS-CoV-2 NSP14 MTase activity is critical for inducing canonical NF-κB activation.Bioscience reports · 2024Article
- Review
- A universal fluorescence polarization high throughput screening assay to target the SAM-binding sites of SARS-CoV-2 and other viral methyltransferases.Emerging microbes & infections · 2023Article
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- The hidden RNA code: implications of the RNA epitranscriptome in the context of viral infections.Frontiers in genetics · 2023Review
- Virtual screening and molecular dynamics simulation for identification of natural antiviral agents targeting SARS-CoV-2 NSP10.Biochemical and biophysical research communications · 2022Article
- Genomics and pathogenesis of the avian coronavirus infectious bronchitis virus.Australian veterinary journal · 2022Review
- A Temperature-Sensitive Recombinant of Avian Coronavirus Infectious Bronchitis Virus Provides Complete Protection against Homologous Challenge.Journal of virology · 2022Article
- High-resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic development.Nature structural & molecular biology · 2022Article
- Replication of the coronavirus genome: A paradox among positive-strand RNA viruses.The Journal of biological chemistry · 2022Review
- Identification of Amino Acids within Nonstructural Proteins 10 and 14 of the Avian Coronavirus Infectious Bronchitis Virus That Result in AttenuationJournal of virology · 2022Article
- High resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic development.Research square · 2022Article
- Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022Review
- Coronaviral RNA-methyltransferases: function, structure and inhibition.Nucleic acids research · 2022Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coronaviruses possess a cap structure at the 5' ends of viral genomic RNA and subgenomic RNAs, which is generated through consecutive methylations by virally encoded guanine-N7-methyltransferase (N7-MTase) and 2'-O-methyltransferase (2'-O-MTase). The coronaviral N7-MTase is unique for its physical linkage with an exoribonuclease (ExoN) harbored in nonstructural protein 14 (nsp14) of coronaviruses. In this study, the structure-function relationships of the N7-MTase were analyzed by deletion and site-directed mutagenesis of severe acute respiratory syndrome coronavirus (SARS-CoV) nsp14. The results showed that the ExoN domain is closely involved in the activity of the N7-MTase, suggesting that coronavirus N7-MTase is different from all other viral N7-MTases, which are separable from other structural domains located in the same polypeptide. Two of the 12 critical residues identified to be essential for the N7-MTase were located at the N terminus of the core ExoN domain, reinforcing a role of the ExoN domain in the N7-MTase activity of nsp14. The other 10 critical residues were distributed throughout the N7-MTase domain but localized mainly in the S-adenosyl-l-methionine (SAM)-binding pocket and key structural elements of the MTase fold of nsp14. The sequence motif DxGxPxA (amino acids [aa] 331 to 338) was identified as the key part of the SAM-binding site. These results provide insights into the structure and functional mechanisms of coronaviral nsp14 N7-MTase.
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