ArticleBiochemical and biophysical research communications2020
Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3.
Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- SARS-CoV-2 nucleocapsid protein variants have differential RNA chaperone activity.The FEBS journal · 2026Article
- Phosphorylation toggles the SARS-CoV-2 nucleocapsid protein between two membrane-associated condensate states.Nature communications · 2025Article
- Impact of mutations on the stability of SARS-CoV-2 nucleocapsid protein structure.Scientific reports · 2024Article
- Article
- Association of SARS-CoV-2 Nucleocapsid Protein Mutations with Patient Demographic and Clinical Characteristics during the Delta and Omicron Waves.Microorganisms · 2023Article
- Intragenomic rearrangements involving 5'-untranslated region segments in SARS-CoV-2, other betacoronaviruses, and alphacoronaviruses.Virology journal · 2023Article
- Association Between ADHD and COVID-19 Infection and Clinical Outcomes: A Retrospective Cohort Study From Electronic Medical Records.Journal of attention disorders · 2023Article
- Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.Journal of structural biology · 2022Article
- Clinical evaluation of the GSD NovaPrime® SARS-CoV-2 RTq-PCR assay.Diagnostic microbiology and infectious disease · 2022Article
- Evolution of SARS-CoV-2 in Spain during the First Two Years of the Pandemic: Circulating Variants, Amino Acid Conservation, and Genetic Variability in Structural, Non-Structural, and Accessory Proteins.International journal of molecular sciences · 2022Article
- SARS CoV-2 (Delta Variant) Infection Kinetics and Immunopathogenesis in Domestic Cats.Viruses · 2022Article
- Phylogenetic analysis of SARS-CoV-2 viruses circulating in the South American region: Genetic relations and vaccine strain match.Virus research · 2022Article
- High diversity in Delta variant across countries revealed by genome-wide analysis of SARS-CoV-2 beyond the Spike protein.Molecular systems biology · 2022Article
- Active site prediction of phosphorylated SARS-CoV-2 N-Protein using molecular simulation.Informatics in medicine unlocked · 2022Article
- Article
- SARS-CoV-2 signaling pathway map: A functional landscape of molecular mechanisms in COVID-19.Journal of cell communication and signaling · 2021Article
- Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins.Biochemical and biophysical research communications · 2021Article
- Epitope mapping of severe acute respiratory syndrome-related coronavirus nucleocapsid protein with a rabbit monoclonal antibody.Virus research · 2021Article
- Mass spectrometry-based proteomic platforms for better understanding of SARS-CoV-2 induced pathogenesis and potential diagnostic approaches.Proteomics · 2021Review
- Antiviral Properties of the NSAID Drug Naproxen Targeting the Nucleoprotein of SARS-CoV-2 Coronavirus.Molecules (Basel, Switzerland) · 2021Article
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2 authors.
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Abstract
SARS-CoV-2 is the etiologic agent of COVID-19. There is currently no effective means of preventing infections by SARS-CoV-2, except through restriction of population movement and contact. An understanding of the origin, evolution and biochemistry (molecular biology) of SARS-CoV-2 is a prerequisite to its control. Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein isolated from various populations and locations, are described. Mutations occurred in the phosphorylation sites, all located within a stretch which forms a phosphorylation dependent interaction site, including C-TAK1 phosphorylation sites for 14-3-3. The consequences of these mutations are discussed and a structure-based model for the role of protein 14-3-3 in the sequestration and inhibition of SARS-CoV-2 nucleocapsid protein's function is presented. It is proposed that the phosphorylation of SARS-CoV-2 nucleocapsid protein and its sequestration by Protein 14-3-3 is a cellular response mechanism for the control and inhibition of the replication, transcription and packaging of the SARS-CoV-2 genome.
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