IndraLab

Statements

USP7 inhibits Ubiquitin. 7 / 7
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"Ubiquitin ligase activity is therefore required for mRNA degradation and can be prevented either by removal of the RING (RINGless MEX-3C) or by overexpression of the USP7 DUB."
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"Importantly, these effects were independent of p53 status and could be rescued by the MG132 proteasome inhibitor, suggesting that USP7 prevents ubiquitin mediated degradation of TRIM27 by the proteaso[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, it is still possible that USP7 may antagonize the action of FBXL21 by cleaving the ubiquitin chain (s) formed by FBXL21."
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"As increased TAL1 oncogenic activity was also evident in the accelerated cell growth observed after CRISPR knock-out of half of the USP7 loci in T-ALL cell lines, we hypothesize that USP7 haploinsufficiency in T-ALL down-regulates the ability of this deubiquitylating enzyme to remove ubiquitin from E-proteins, leads to enhanced TAL1 heterodimer formation, which favors TAL1 mediated thymocyte transformation."
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"This class of allosteric inhibitors has been demonstrated to bind to the ' palm ' region of the USP7 catalytic domain thereby impeding ubiquitin binding (orange, XREF_FIG) [XREF_BIBR, XREF_BIBR]."
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"Importantly, these effects were independent of p53 status and could be rescued by the MG132 proteasome inhibitor (XREF_FIG), suggesting that USP7 prevents ubiquitin mediated degradation of TRIM27 by the proteasome."
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"Although USP7, like all DUBS, deconjugates ubiquitin from several target proteins, inhibition of USP7 promotes the degradation of its primary cellular target, HDM2, resulting in net p53 stabilization and activation [30, 42, 43] ."
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