IndraLab

Statements

USP7 activates EBNA1. 7 / 7
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"This suggests that USP7 inhibition impairs the half‐life of EBNA1 and the effects of USP7 inhibitors are likely to affect EBNA1 protein stability.To confirm that the observations were not a product of off‐target effects by the inhbitors, we performed siRNA knockdown specifically against USP7 in EBV gastric cell line YCCEL1."
39821265
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"Therefore we conclude that USP7 can stimulate the assembly of EBNA1 on oriP elements in vivo."
19834552
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"In keeping with this hypothesis, we found that USP7 within this complex can mediate an interaction with GMPS which promotes deubiquitylation of histone H2B and that USP7 contributes to EBNA1 mediated transcriptional activation."
19834552
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"However we have also shown that USP7 can stimulate the assembly of EBNA1 on oriP elements in transfected plasmids suggesting that USP7 might play a role in the initial association of EBNA1 with these elements upon initial EBV infection, and/or during the switch from the EBV latency form in nonproliferating cells, in which EBNA1 is not expressed, to latency forms in proliferating cells in which EBNA1 is expressed and bound to oriP."
19834552
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"In conclusion, our findings indicate that pharmacological inhibition of USP7 impairs EBNA1 function and EBV‐driven cell growth, and that USP7 is an attractive candidate for EBV‐targeted therapy."
39821265
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"While stoichiometric amounts of USP7 were sufficient to stimulate the DNA binding activity of EBNA1, only at higher USP7 concentrations was USP7 observed to be stably associated with the EBNA1 and DNA complex in vitro."
19834552
reach
"USP7 also contributes to EBNA1 mediated transcriptional activation and stimulates the assembly of EBNA1 on oriP elements in transfected plasmids [XREF_BIBR]."
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