ArticleBiochemical and biophysical research communications2008
The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- Nucleolar Protein Treacle Is Important for the Efficient Growth of Mumps Virus.Journal of virology · 2022Article
- Identification of 1,2,3-triazole-phthalimide derivatives as potential drugs against COVID-19: a virtual screening, docking and molecular dynamic study.Journal of biomolecular structure & dynamics · 2022Article
- Identification of a guanine-specific pocket in the protein N of SARS-CoV-2.Communications biology · 2022Article
- The status and analysis of common mutations found in the SARS-CoV-2 whole genome sequences from Bangladesh.Gene reports · 2022Article
- Targeting CK2 mediated signaling to impair/tackle SARS-CoV-2 infection: a computational biology approach.Molecular medicine (Cambridge, Mass.) · 2021Article
- Exploiting the molecular basis of age and gender differences in outcomes of SARS-CoV-2 infections.Computational and structural biotechnology journal · 2021Article
- Role of Host-Mediated Post-Translational Modifications (PTMs) in RNA Virus Pathogenesis.International journal of molecular sciences · 2020Review
- SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs.The EMBO journal · 2020Article
- Molecular mechanisms of the novel coronavirus SARS-CoV-2 and potential anti-COVID19 pharmacological targets since the outbreak of the pandemic.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2020Review
- Structural Proteins in Severe Acute Respiratory Syndrome Coronavirus-2.Archives of medical research · 2020Review
- SARS-CoV-2 nucleocapsid protein undergoes liquid-liquid phase separation stimulated by RNA and partitions into phases of human ribonucleoproteins.bioRxiv : the preprint server for biology · 2020Article
- Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.Frontiers in chemistry · 2020Review
- Review
- Viruses and the nucleolus: the fatal attraction.Biochimica et biophysica acta · 2014Article
- Article
- The SARS coronavirus nucleocapsid protein--forms and functions.Antiviral research · 2014Review
- Human coronavirus OC43 nucleocapsid protein binds microRNA 9 and potentiates NF-κB activation.Journal of virology · 2014Article
- The evolutionary significance of depression in Pathogen Host Defense (PATHOS-D).Molecular psychiatry · 2013Article
- Involvement of the nucleolus in replication of human viruses.Reviews in medical virology · 2009Review
- Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.