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http://purl.uniprot.org/citations/32829876 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2020.08.024"xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/author | "Limtung P."xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/author | "Tung H.Y.L."xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/pages | "134-138"xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/title | "Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3."xsd:string |
http://purl.uniprot.org/citations/32829876 | http://purl.uniprot.org/core/volume | "532"xsd:string |
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