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10.3390/v12040384

http://scihub22266oqcxt.onion/10.3390/v12040384
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32244383!7232374!32244383
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suck abstract from ncbi


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pmid32244383      Viruses 2020 ; 12 (4): ä
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  • The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation #MMPMID32244383
  • Alhammad YMO; Fehr AR
  • Viruses 2020[Mar]; 12 (4): ä PMID32244383show ga
  • Macrodomains, enzymes that remove ADP-ribose from proteins, are encoded by several families of RNA viruses and have recently been shown to counter innate immune responses to virus infection. ADP-ribose is covalently attached to target proteins by poly-ADP-ribose polymerases (PARPs), using nicotinamide adenine dinucleotide (NAD+) as a substrate. This modification can have a wide variety of effects on proteins including alteration of enzyme activity, protein-protein interactions, and protein stability. Several PARPs are induced by interferon (IFN) and are known to have antiviral properties, implicating ADP-ribosylation in the host defense response and suggesting that viral macrodomains may counter this response. Recent studies have demonstrated that viral macrodomains do counter the innate immune response by interfering with PARP-mediated antiviral defenses, stress granule formation, and pro-inflammatory cytokine production. Here, we will describe the known functions of the viral macrodomains and review recent literature demonstrating their roles in countering PARP-mediated antiviral responses.
  • |ADP-Ribosylation/*immunology[MESH]
  • |Adenosine Diphosphate Ribose/metabolism[MESH]
  • |Cytoplasmic Granules/immunology/virology[MESH]
  • |Humans[MESH]
  • |Interferons/immunology[MESH]
  • |Mutation[MESH]
  • |Poly(ADP-ribose) Polymerases/immunology[MESH]
  • |Protein Domains[MESH]
  • |RNA Virus Infections/immunology/metabolism/virology[MESH]
  • |RNA Viruses/classification/genetics/*immunology/metabolism[MESH]
  • |Viral Nonstructural Proteins/*chemistry/genetics/*immunology/metabolism[MESH]


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