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10.3390/v14030611

http://scihub22266oqcxt.onion/10.3390/v14030611
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35337019!8951556!35337019
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suck abstract from ncbi


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pmid35337019      Viruses 2022 ; 14 (3): ä
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  • A BioID-Derived Proximity Interactome for SARS-CoV-2 Proteins #MMPMID35337019
  • May DG; Martin-Sancho L; Anschau V; Liu S; Chrisopulos RJ; Scott KL; Halfmann CT; Diaz Pena R; Pratt D; Campos AR; Roux KJ
  • Viruses 2022[Mar]; 14 (3): ä PMID35337019show ga
  • The novel coronavirus SARS-CoV-2 is responsible for the ongoing COVID-19 pandemic and has caused a major health and economic burden worldwide. Understanding how SARS-CoV-2 viral proteins behave in host cells can reveal underlying mechanisms of pathogenesis and assist in development of antiviral therapies. Here, the cellular impact of expressing SARS-CoV-2 viral proteins was studied by global proteomic analysis, and proximity biotinylation (BioID) was used to map the SARS-CoV-2 virus-host interactome in human lung cancer-derived cells. Functional enrichment analyses revealed previously reported and unreported cellular pathways that are associated with SARS-CoV-2 proteins. We have established a website to host the proteomic data to allow for public access and continued analysis of host-viral protein associations and whole-cell proteomes of cells expressing the viral-BioID fusion proteins. Furthermore, we identified 66 high-confidence interactions by comparing this study with previous reports, providing a strong foundation for future follow-up studies. Finally, we cross-referenced candidate interactors with the CLUE drug library to identify potential therapeutics for drug-repurposing efforts. Collectively, these studies provide a valuable resource to uncover novel SARS-CoV-2 biology and inform development of antivirals.
  • |*COVID-19[MESH]
  • |*SARS-CoV-2[MESH]
  • |Biotinylation[MESH]
  • |Humans[MESH]
  • |Pandemics[MESH]


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