IndraLab

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USP40 deubiquitinates HSP90. 7 / 7
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"USP40 overexpression increased lysine acetylation of HSP90β (Fig. 6i, j), suggesting that USP40 deubiquitinates HSP90β, resulting in an increase in lysine acetylation of HSP90β, thereby leading to inactivation of HSP90β and preservation of EC integrity."
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"We revealed that USP40 preserves EC function by deubiquitinating and inactivating HSP90β."
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"USP40 deubiquitinates HSP90β, resulting in the inactivation of HSP90β in ECs, suggesting that USP40 protects EC integrity by blocking HSP90β-mediated EC dysfunction."
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"Taken together with findings showing that USP40 deubiquitinates HSP90β, these data suggest that USP40 inactivates HSP90β by modulating its ubiquitination and acetylation.The detrimental effect of HSP90 activity in ECs has been well reported ."
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"This is the first report to reveal that USP40 deubiquitinates and inactivates HSP90."
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"Taken together, this study shows that USP40 deubiquitinates HSP90β, thereby inhibiting its activity by increasing its acetylation (Fig. 7g)."
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"Furthermore, our data reveal that USP40 deubiquitinates HSP90, thereby increasing its acetylation and reducing its activation."
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