ArticleBiomolecular NMR assignments2016
NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV).
Article in Biomolecular NMR assignments, 2016. 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.
- NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS-CoV and MERS-CoV MDs in the free and the ADPr-bound state.Biomolecular NMR assignments · 2022Article
- Article
- Elucidating the tunability of binding behavior for the MERS-CoV macro domain with NAD metabolites.Communications biology · 2021Article
- Molecular Characteristics, Functions, and Related Pathogenicity of MERS-CoV Proteins.Engineering (Beijing, China) · 2019Review
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4 authors.
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Abstract
The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangible about their exact function. In this study we report the preliminary structural analysis through solution NMR spectroscopy of the MERS-CoV macro domain. The near complete NMR assignments of MERS-CoV macro domain provide the basis for subsequent structural and biochemical investigation in the context of protein function.
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