IndraLab

Statements


USP3 activates DDR. 4 / 4
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"Isolation of USP3 interacting partners and potential additional substrates, as well as addressing if and how USP3 is regulated, is needed to gain a better understanding of the molecular mechanism of USP3 mediated DDR."

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"Overall, despite the non-specificity towards H2A ubiquitination [74], current data support the notion that USP3, at least in part, counteracts the RNF168-mediated pathway in regulating the DDR."

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"Knockdown of USP3 impairs the DDR through SMARCA5 and results in increased sensitivity to Docetaxel treatment in prostate cancer cells."

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"38 Conversely, Das et al. report that the upregulation of USP3 stimulates the DDR, evident from a substantial increase in γ‐H2AX following USP3 overexpression."