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- W4361268253 abstract "Tumor development relies on a complex and aberrant tissue environment in which cancer cells receive the necessary nutrients for growth, survive through immune escape, and acquire mesenchymal properties that mediate invasion and metastasis. Stromal cells and soluble mediators in the tumor microenvironment (TME) exhibit characteristic anti-inflammatory and protumorigenic activities. Ubiquitination, which is an essential and reversible posttranscriptional modification, plays a vital role in modulating the stability, activity and localization of modified proteins through an enzymatic cascade. This review was motivated by accumulating evidence that a series of E3 ligases and deubiquitinases (DUBs) finely target multiple signaling pathways, transcription factors and key enzymes to govern the functions of almost all components of the TME. In this review, we systematically summarize the key substrate proteins involved in the formation of the TME and the E3 ligases and DUBs that recognize these proteins. In addition, several promising techniques for targeted protein degradation by hijacking the intracellular E3 ubiquitin-ligase machinery are introduced." @default.
- W4361268253 created "2023-03-31" @default.
- W4361268253 creator A5002843546 @default.
- W4361268253 creator A5007113758 @default.
- W4361268253 creator A5055092586 @default.
- W4361268253 creator A5060643969 @default.
- W4361268253 creator A5075122118 @default.
- W4361268253 creator A5079040033 @default.
- W4361268253 creator A5082402921 @default.
- W4361268253 creator A5091241974 @default.
- W4361268253 date "2023-03-30" @default.
- W4361268253 modified "2023-10-18" @default.
- W4361268253 title "Exploiting E3 ubiquitin ligases to reeducate the tumor microenvironment for cancer therapy" @default.
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