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10.1016/j.bbrc.2020.08.024

http://scihub22266oqcxt.onion/10.1016/j.bbrc.2020.08.024
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32829876!7428706!32829876
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suck abstract from ncbi


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pmid32829876      Biochem+Biophys+Res+Commun 2020 ; 532 (1): 134-138
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  • Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3 #MMPMID32829876
  • Tung HYL; Limtung P
  • Biochem Biophys Res Commun 2020[Oct]; 532 (1): 134-138 PMID32829876show ga
  • 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.
  • |*Genome, Viral[MESH]
  • |14-3-3 Proteins/*chemistry/genetics/metabolism[MESH]
  • |Amino Acid Sequence[MESH]
  • |Betacoronavirus/*genetics/metabolism/pathogenicity[MESH]
  • |Binding Sites[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/virology[MESH]
  • |Coronavirus Nucleocapsid Proteins[MESH]
  • |Gene Expression[MESH]
  • |Host-Pathogen Interactions/*genetics[MESH]
  • |Humans[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Mutation[MESH]
  • |Nucleocapsid Proteins/*chemistry/genetics/metabolism[MESH]
  • |Pandemics[MESH]
  • |Phosphoproteins[MESH]
  • |Phosphorylation[MESH]
  • |Pneumonia, Viral/virology[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation, alpha-Helical[MESH]
  • |Protein Conformation, beta-Strand[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |Protein Multimerization[MESH]
  • |SARS-CoV-2[MESH]
  • |Sequence Alignment[MESH]
  • |Sequence Homology, Amino Acid[MESH]


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