| Links between the oncoprotein YB-1 and small non-coding RNAs in breast cancer. | breast, |
| C1QBP negatively regulates the activation of oncoprotein YBX1 in the renal cell carcinoma as revealed by interactomics analysis. | kidney, |
| These findings demonstrate the oncogenic roles of YB-1 in esophageal squamous cell carcinoma (ESCC) and support it as a target for ESCC therapy. | esophageal, |
| Data suggest that oncogenic Y-box binding protein 1 (YB-1) indirectly enhances transforming growth factor beta (TGFbeta) signaling cascades via Sma/Mad related protein 2 (Smad2)phospho-activation and may represent a promising factor for future diagnosis and therapy of breast cancer. | breast, |
| Analysis of 918 lung cancer and normal lung tissues and lung cancer cell lines revealed that MIR22HG was significantly downregulated in lung cancer; this decreased expression was associated with poor patient survival. MIR22HG bound and stabilized the YBX1 protein. Silencing of MIR22HG triggered both cell survival and cell death signaling through dysregulation of the oncogenes YBX1, MET, and p21. | lung, |
| Phosphorylation by Akt disables the anti-oncogenic activity of YB-1. | None |
| Genotoxic stress-induced nuclear localization of oncoprotein YB-1 in the absence of proteolytic processing. | None |
| Ionizing radiation induces YB-1 phosphorylation. YB-1 phosphorylation induced by oncogenic K-Ras or IR enhances repair of DNA-double stranded breaks and postirradiation survival via erbB1 downstream PI3K/Akt and MAPK/ERK signaling pathways. | None |
| The mechanisms of regulation of YB-1 expression in the cell, the involvement of YB-1 in oncogenic cell transformation, multiple drug resistance, and dissemination of tumors are reviewed. [Review] | None |
| YB-1: oncoprotein, prognostic marker and therapeutic target?. | None |
| Cell fate factor DACH1 represses YB-1-mediated oncogenic transcription and translation. | None |
| Cell fate factor DACH1 represses YB-1-mediated oncogenic transcription and translation. | None |
| Study reveals that a specific set of tRNA-derived fragments functionally engage the oncogenic RNA-binding protein YBX1. These fragments, which contain a CU box motif, post-transcriptionally suppress the expression of YBX1 transcripts by competitively displacing them from YBX1. | None |