Selected article for: "formation suppress and SG formation"
Author: Aravinth Kumar Jayabalan; Diane E. Griffin; Anthony K. L. Leung
Title: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation
  • Document date: 2019_6_20
    • ID: n8sjpcbs_11
    Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/629881 doi: bioRxiv preprint Page 7 arsenite treatment (Fig. 1a, asterisk) . In cells transfected with full-length nsP3, nsP3 co-localized with G3BP1, but not with eIF3b in the majority of cells examined (73%; Fig. 1a , c), as previously reported [36, 42] . In contrast, in cells transfected with the nsP3 HVD alone, the nsP3 HVD co-.....
    Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/629881 doi: bioRxiv preprint Page 7 arsenite treatment (Fig. 1a, asterisk) . In cells transfected with full-length nsP3, nsP3 co-localized with G3BP1, but not with eIF3b in the majority of cells examined (73%; Fig. 1a , c), as previously reported [36, 42] . In contrast, in cells transfected with the nsP3 HVD alone, the nsP3 HVD co-localized with both SG components eIF3b and G3BP1 in 93% of cells examined (Fig. 1a, c) . These data indicate that HVD alone cannot suppress SG formation, but instead the domain associates with SG proteins.

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