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USP4 activates apoptotic process. 15 / 16
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"However, in response to cisplatin treatment, USP4 deficiency significantly augmented melanoma cells apoptosis by activating p53 signalling."
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"The silencing of USP4 can inhibit the apoptosis of cancer cells and increase the persistent survival rate of HNSCC, as immunosuppressive diseases, UXP9X, CYLD1, and BPLF1 accelerate the development of HNSCC through the escape inhibition mechanism of immune cells or promoting the spread of virus infection."
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"Consistent with this, the results of Hou et al. 28 showed that USP4 promotes apoptosis and inhibits NF-kappaB activation in head and neck squamous cell carcinoma."
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"Apoptosis related protein Bax, Cleaved caspase-3 expression was increased, and Bcl2, caspase-3 expression was decreased (Fig. 3D), indicating that USP4 could promote cell apoptosis and inhibit cell proliferation."
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"However, in response to cisplatin induced stress, the knockdown of USP4 could markedly increase the apoptotic rate of melanoma cells, and USP4 deficiency sensitized melanoma cell to cisplatin induced apoptosis by activating p53 pathway."
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"USP4 might negatively regulates RIP1-mediated NF-κB activation and promotes TNF-α-induced apoptosis in FaDu cells, as well as directly interacted with receptor-interacting protein 1 (RIP1) and deubiquitinated K63-linked ubiquitination from RIP142."
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"We subsequently showed that USP4 regulated cisplatin induced cell apoptosis via p53 signalling."
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"The overexpression of USP4 in HNSCC tissues may be modulated by host immune cells to promote apoptosis of cancer cells and attenuate cancer progression."
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"The findings showed that the expression of TGF-betaR1 and USP4 were increased in hypertrophic scar tissues and fibroblasts, and that down-regulating USP4 inhibited hypertrophic scar fibroblast proliferation and migration and induced cell apoptosis in vitro."
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"As shown in Fig. 2 B, USP4 overexpression significantly promotes cell apoptosis in FaDu cells in responses to TNF-α with CHX."
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"In contrast, the USP4 point mutant (C311S) without deubiquitinase activity lost the ability to promote cell apoptosis ( Fig. 2 B), indicating deubiquitinase activity is required for the USP4-mediated [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP4 knockdown in FaDu cells repressed cell apoptosis ( Fig. 2 E)."
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"In this study, we demonstrate that USP4 is upregulated in HNSCC and promotes TNF-α-induced apoptosis by targeting RIP1 for deubiquitination."
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"USP4 knockout mice exhibited exacerbated hepatic I/R injury, as evidenced by enhanced liver inflammation via the NF-kappaB signalling pathway and increased hepatocyte apoptosis."
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"In this study, we demonstrate that de-ubiquitinating protease USP4 negatively regulates RIP1-mediated NF-κB activation and promotes TNF-α-induced apoptosis through interacting with RIP1 and deubiquiti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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