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http://purl.uniprot.org/citations/32829876http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32829876http://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/32829876http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2020.08.024"xsd:string
http://purl.uniprot.org/citations/32829876http://purl.uniprot.org/core/author"Limtung P."xsd:string
http://purl.uniprot.org/citations/32829876http://purl.uniprot.org/core/author"Tung H.Y.L."xsd:string
http://purl.uniprot.org/citations/32829876http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32829876http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/32829876http://purl.uniprot.org/core/pages"134-138"xsd:string
http://purl.uniprot.org/citations/32829876http://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/32829876http://purl.uniprot.org/core/volume"532"xsd:string
http://purl.uniprot.org/citations/32829876http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32829876
http://purl.uniprot.org/citations/32829876http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32829876
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http://purl.uniprot.org/uniprot/#_P27348-mappedCitation-32829876http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32829876
http://purl.uniprot.org/uniprot/#_Q53RR5-mappedCitation-32829876http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32829876
http://purl.uniprot.org/uniprot/#_Q53S41-mappedCitation-32829876http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32829876
http://purl.uniprot.org/uniprot/B4DMT8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32829876
http://purl.uniprot.org/uniprot/Q53S41http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32829876
http://purl.uniprot.org/uniprot/P27348http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32829876
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http://purl.uniprot.org/uniprot/B4DY04http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32829876