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• W2904342249 abstract "Cells mainly rely on stress proteins, such as heat-shock proteins (HSPs), to respond to various proteotoxic conditions. These proteins protect tumor cells and enhance their survive. However, the regulation of stress proteins involved in protein quality control (PQC) is still poorly understood. Here, we report that the expression of TRIM11, an important regulator of PQC, is positively correlated with tumor cell surviaval during the proteotoxic conditions induced by anti-tumor drugs. In addition, HSF1 is required for TRIM11-mediated removal of protein aggregates and resistance of proteotoxic stress. During these processes, TRIM11 interacts with and stabilizes HSF1, increaseing HSF1 levels in the nucleus. These findings identify that TRIM11, through cooperation with HSF1, protects cells against the proteotoxic stress and promotes tumor cell survival." @default.
• W2904342249 created "2018-12-22" @default.
• W2904342249 creator A5062750514 @default.
• W2904342249 creator A5082464514 @default.
• W2904342249 date "2018-12-26" @default.
• W2904342249 modified "2023-10-12" @default.
• W2904342249 title "TRIM11 cooperates with HSF1 to suppress the anti-tumor effect of proteotoxic stress drugs" @default.
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• W2904342249 doi "https://doi.org/10.1080/15384101.2018.1558870" @default.
• W2904342249 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6343683" @default.
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