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10.1096/fj.202001351

http://scihub22266oqcxt.onion/10.1096/fj.202001351
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32562316!7323129!32562316
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suck abstract from ncbi


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pmid32562316      FASEB+J 2020 ; 34 (8): 9832-9842
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  • A proposed role for the SARS-CoV-2 nucleocapsid protein in the formation and regulation of biomolecular condensates #MMPMID32562316
  • Cascarina SM; Ross ED
  • FASEB J 2020[Aug]; 34 (8): 9832-9842 PMID32562316show ga
  • To date, the recently discovered SARS-CoV-2 virus has afflicted >6.9 million people worldwide and disrupted the global economy. Development of effective vaccines or treatments for SARS-CoV-2 infection will be aided by a molecular-level understanding of SARS-CoV-2 proteins and their interactions with host cell proteins. The SARS-CoV-2 nucleocapsid (N) protein is highly homologous to the N protein of SARS-CoV, which is essential for viral RNA replication and packaging into new virions. Emerging models indicate that nucleocapsid proteins of other viruses can form biomolecular condensates to spatiotemporally regulate N protein localization and function. Our bioinformatic analyses, in combination with pre-existing experimental evidence, suggest that the SARS-CoV-2 N protein is capable of forming or regulating biomolecular condensates in vivo by interaction with RNA and key host cell proteins. We discuss multiple models, whereby the N protein of SARS-CoV-2 may harness this activity to regulate viral life cycle and host cell response to viral infection.
  • |Binding Sites[MESH]
  • |Computational Biology[MESH]
  • |Coronavirus Nucleocapsid Proteins/*chemistry[MESH]
  • |Cytoplasmic Granules/chemistry[MESH]
  • |Humans[MESH]
  • |Phosphoproteins/chemistry[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Protein Kinases/chemistry[MESH]
  • |SARS-CoV-2/*chemistry/physiology[MESH]
  • |Virus Assembly[MESH]


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