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OTUD5 inhibits ferroptosis. 10 / 10
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"Collectively, our data illustrate that 4‐HNE triggers ubiquitin–proteasomal degradation of GPX4 in cardiomyocytes.2.5 OTUD5 Mediates 4-HNE-Induced GPX4 Degradation and Ferroptosis."
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"p53 inhibits OTUD5 transcription to promote GPX4 degradation and induce ferroptosis in gastric cancer."
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"These findings demonstrate that both OTUD5 knockdown and nutlin‐3a treatment can induce ferroptosis and suppress cell proliferation."
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"To evaluate whether OTUD5 inhibited ferroptosis, we assessed the levels of iron, MDA, and GSH (Figure 7E,F; Figure S9B, Supporting Information)."
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"Additionally, OTUD5 silencing and nutlin-3a-induced GPX4 degradation enhances the sensitivity of gastric cancer cells to ferroptosis in vivo."
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"We treated control and OTUD5‐KO cells with nutlin‐3a and observed that knockout of OTUD5, in combination with nutlin‐3a treatment, led to a reduction in protein levels of OTUD5 and GPX4 (Figure 5A,B), thereby triggering ferroptosis in cancer cells and consequently inhibiting cell proliferation (Figure 5C,D)."
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"Upregulation of OTUD5 deubiquitinates and stabilizes GPX4, thus reversing 4-HNE-induced ferroptosis and alleviating myocardial I/R injury [96]."
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"Conversely, in gastric cancer cells harbouring p53 mutations, OTUD5 transcription is upregulated due to the inactivation of p53, allowing OTUD5 to stabilise GPX4 protein, inhibit ferroptosis and thereby promoting gastric cancer progression (Figure 6J, right panel)."
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"In conclusion, these results demonstrated that OTUD5 mediates the K48‐linked deubiquitination of GPX4 and stabilises GPX4.2.3 OTUD5 suppresses ferroptosis via GPX4."
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"OTUD5 inhibited ferroptosis and alleviated myocardial injury by directly binding to glutathione peroxidase 4 (GPX4), the key protein of ferroptosis, and removing the K48-linked ubiquitin chains of GPX4 (Ref."
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