ArticleThe Journal of biological chemistry2026
Structural basis of DNA aptamer A58 targeting the N-terminal domain of sarbecoviruses nucleocapsid protein.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed.
- AptViralDB: A repository of experimentally validated antiviral aptamers.Molecular therapy. Nucleic acids · 2026Review
- The Intrinsic Disordered N-Terminus of Nucleocapsid Protein of SARS-CoV-2 Is Critical in DNA Aptamer Binding.International journal of molecular sciences · 2026Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the post-pandemic era, the persistent threat of coronaviruses demands broad-spectrum antiviral therapeutic strategies. The SARS-CoV-2 nucleocapsid protein (N protein), an essential factor for genome packaging and immune modulation, poses a promising antiviral target. Here, we determined the crystal structure of the DNA aptamer A58-T10 in complex with the N-terminal domain of the N protein (N-NTD). A58-T10 binds to the N-NTD via a unique three-tiered stem-loop that interacts with the nucleic acid-binding site of N-NTD through extensive hydrogen bonding and stacking. Structural analysis reveals that A58 contains two stem-loops with octanucleotide motifs (5'-
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