IndraLab

Statements


USP13 deubiquitinates PTEN. 8 / 8
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"Therefore, USP13 can directly deubiquitinate PTEN."

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"Wild-type USP13 purified from either bacteria or 293T cells, but not its catalytically inactive mutant C345A, decreased PTEN poly-ubiquitination by 64-70% in vitro (XREF_FIG)."

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"USP13 deubiquitinates and stabilizes PTEN."

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"Deubiquitination and stabilization of PTEN by USP13."

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"Deubiquitination of PTEN by USP13, a deubiquitinating enzyme, stabilized PTEN, and thereby inhibited breast cancer tumorigenesis [5]."

"Deubiquitylation and stabilization of PTEN by USP13"

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"Deubiquitylation and stabilization of PTEN by USP13."

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"On the other hand, ectopic expression of wild-type USP13, but not the C345A mutant which is still capable of interacting with PTEN (XREF_FIG), reduced the poly-ubiquitination of PTEN by 65% (XREF_FIG), suggesting that the enzymatic activity of USP13 is indispensable for USP13 dependent deubiquitination of PTEN."