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_30
Snippet: To determine whether the ADP-ribosylhydrolase activity can also cause the dissolution of preformed FUS R495X-induced aggregates, we transfected the FUS R495X construct 12 h prior to the nsP3 constructs (Fig. 3d) . As in the case for co-transfection, transfection of WT nsP3 or MD alone, but not G32E nsP3, decreased the number of aggregates by at least 2.5-fold (Fig. 3d-e) . These data suggest that the SG-like aggregates induced by FUS R495X can al.....
Document: To determine whether the ADP-ribosylhydrolase activity can also cause the dissolution of preformed FUS R495X-induced aggregates, we transfected the FUS R495X construct 12 h prior to the nsP3 constructs (Fig. 3d) . As in the case for co-transfection, transfection of WT nsP3 or MD alone, but not G32E nsP3, decreased the number of aggregates by at least 2.5-fold (Fig. 3d-e) . These data suggest that the SG-like aggregates induced by FUS R495X can also be disrupted by nsP3 ADPribosylhydrolase activity.
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