ArticleFEBS letters2013
Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.
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Who cites it
58 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.
- Drug targets for corona virus: A systematic review.Indian journal of pharmacologyPooled it
- Article
- Coronavirus genome packaging and nucleocapsid assembly.Journal of virology · 2026Review
- Characterization of the binding features between SARS-CoV-2 5'-proximal transcripts of genomic RNA and nucleocapsid proteins.RNA biology · 2025Review
- Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SARS-CoV-2 papain-like protease inhibits ISGylation of the viral nucleocapsid protein to evade host anti-viral immunity.Journal of virology · 2024Article
- ISGylation of the SARS-CoV-2 N protein by HERC5 impedes N oligomerization and thereby viral RNA synthesis.Journal of virology · 2024Article
- SARS-CoV-2 Nucleocapsid Protein Induces Tau Pathological Changes That Can Be Counteracted by SUMO2.International journal of molecular sciences · 2024Article
- ISGylation of the SARS-CoV-2 N protein by HERC5 impedes N oligomerization and thereby viral RNA synthesis.bioRxiv : the preprint server for biology · 2024Article
- A narrow ratio of nucleic acid to SARS-CoV-2 N-protein enables phase separation.bioRxiv : the preprint server for biology · 2024Article
- Targeting protein-protein interaction interfaces with antiviral N protein inhibitor in SARS-CoV-2.Biophysical journal · 2024Article
- Aptamers targeting SARS-CoV-2 nucleocapsid protein exhibit potential anti pan-coronavirus activity.Signal transduction and targeted therapy · 2024Article
- Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024Review
- Comparative genomics of spike, envelope, and nucleocapsid protein of severe acute respiratory syndrome coronavirus 2.African health sciences · 2023Article
- A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins.Science advances · 2023Article
- Classification, replication, and transcription ofFrontiers in microbiology · 2023Review
- Contributions of the N-terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA-induced phase separation.Protein science : a publication of the Protein Society · 2022Article
- Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.Journal of the American Chemical Society · 2022Article
- Structural dynamics of SARS-CoV-2 nucleocapsid protein induced by RNA binding.PLoS computational biology · 2022Article
- The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a.Science advances · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coronavirus (CoV) N protein oligomerizes via its carboxyl terminus. However, the oligomerization mechanism of the C-terminal domains (CTD) of CoV N proteins remains unclear. Based on the protein disorder prediction system, a comprehensive series of HCoV-229E N protein mutants with truncated CTD was generated and systematically investigated by biophysical and biochemical analyses to clarify the role of the C-terminal tail of the HCoV-229E N protein in oligomerization. These results indicate that the last C-terminal tail plays an important role in dimer-dimer association. The C-terminal tail peptide is able to interfere with the oligomerization of the CTD of HCoV-229E N protein and performs the inhibitory effect on viral titre of HCoV-229E. This study may assist the development of anti-viral drugs against HCoV.
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