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USP7 deubiquitinates CHFR. 7 / 7
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"These results demonstrate that USP7 preferentially functions in deubiquitination of Chfr, and prevents autoubiquitination mediated degradation of Chfr.The present study has demonstrated that Chfr bind[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"It is reported that USP7 can mediate the deubiquitination of CHFR protein, and the E3 enzyme activity of CHFR protein can target Aurora-A kinase for ubiquitination-dependent protein degradation."

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"For example, USP7 mediates the deubiquitination of the checkpoint protein CHFR."

"In this study, we identified USP7 (also known as HAUSP), which is a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors, as an interacting protein with Chfr by immunoaffinity purification and mass spectrometry, and their interaction greatly increases the stability of Chfr. In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated Chfr both in vivo and in vitro, which results in the accumulation of Chfr in the cell.  USP7 mediates deubiquitination of Chfr."

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"Ubiquitin specific protease, USP7 and HAUSP deubiquitinates CHFR and prevents its degradation, resulting in the increased stability [9]."

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"Thus, we examined whether USP7 can mediate the deubiquitination of Chfr in vivo."