IndraLab

Statements



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"Zhao et al. further indicated that USP39 promoted the proliferation of ESCC cells by enhancing the splicing and maturation of Rictor mRNA, a component of the mTOR complex, and regulating the mTORC2 signaling pathway [50]."

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"Moreover, USP39 activated PI3K/AKT/HIF-1alpha signaling pathway via interacting with and stabilizing PGK1 to stimulate glycolysis."

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"Mechanistically, histone lactylation promoted the expression of ubiquitin-specific peptidase 39 (USP39), which interacted with, stabilized, and de-ubiquitinated phosphoglycerate kinase 1 (PGK1), thereby activating the PI3K/AKT/HIF-1α signaling pathway."

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"In turn, histone lactylation regulated the expression of USP39, and USP39 activated the PI3K/AKT/HIF-1α signaling pathway by interacting with PGK1."

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"Here, we prove that USP39 promotes HCC cell proliferation and migration by directly deubiquitin beta-catenin, a key molecular of Wnt/beta-catenin signaling pathway whose abnormal expression or activation results in several tumors, following its co-localization with USP39."

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"Histone lactylation and USP39 accelerate glycolysis by activating the PI3K/AKT/HIF-1alpha signaling pathway in EC."

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"Previous studies have reported that USP39 silencing inhibits colon cancer cell growth and metastasis, and induces apoptosis by regulating the Wnt/β-catenin signaling pathway [31]."