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The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

GSE281983 Mus musculus Expression profiling by high throughput sequencing 6 samples Submitted 2025/04/22 Platform GPL24247
Summary
Ubiquitin-specific peptidase 24 (USP24), a cysteine protease, functions as deubiquitinating enzyme that recognizes and removes ubiquitin from the target protein. USP24 is overexpressed in various cancers and regulates the stability of proteins involved in cancer metastasis, cancer stemness, and drug resistance. While the expression profile alteration in tumor microenvironment upon USP24 inhibition is unrevealed. Through RNA-seq, we have characterized that USP24 catalytically inactivation upregulates activation of immune response and lymphocyte activation-related genes in lung tumors from EgfrL858RUsp24C1695A mice
Published in
Deubiquitinase USP24 activated by IL-6/STAT3 enhances PD-1 protein stability and suppresses T cell antitumor response
Hsieh HC, Young MJ, Chen KY et al. · Science advances 2025 · PMID 40238877 · doi:10.1126/sciadv.adt4258
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Also filed as BioProject PRJNA1186555 and SRA study SRP545421. Searching any of these in the dataset finder brings you back here.

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