IndraLab

Statements

USP10 binds RNF168. 9 / 9
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sparser
"Finally, we show that the deubiquitylase USP10 interacts with RNF168 and TOP2α, and restrains ubiquitylation of TOP2α as well as its chromatin binding."
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sparser
"Therefore, interactions between USP10, RNF168, and TOP2α may play a key role in the development of tumor resistance to TOP2 inhibitors ( xref )."
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biogrid
No evidence text available
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biogrid
No evidence text available
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reach
"These novel functional interactions between RNF168, TOP2alpha and USP10 are likely to contribute to the maintenance of chromosomal integrity."
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reach
"Finally, we show that the deubiquitylase USP10 interacts with RNF168 and TOP2alpha, and restrains ubiquitylation of TOP2alpha as well as its chromatin binding."
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biogrid
No evidence text available
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sparser
"Indeed, IP/IB analysis confirmed interaction of USP10 with RNF168 ( xref )."
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sparser
"USP10 interacts with RNF168 and TOP2α to inhibit ubiquitination and chromatin binding of TOP2α [59] ."
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