Fig. 2
From: o8G-modified circKIAA1797 promotes lung cancer development by inhibiting cuproptosis
YBX1 acts as an o8G reader to increase circKIAA1797 stability. (A and B) Results of circKIAA1797 o8G RIP-qPCR and agarose gel electrophoresis. (C) Results of circKIAA1797 o8G-modified CLIP-qPCR. (D) Detection of intracellular ROS levels by flow cytometry after the treatment of cells with 0 nM, 100 nM, 200 nM, 300 nM and 400 nM H2O2. (E) Flow cytometry detection of intracellular ROS levels after the treatment of cells with 0 mM, 1 mM, 2 mM, or 5 mM H2O2. (F) Three groups of samples were established, namely, the untreated NC control group, H2O2 -treated group, and NAC-treated group, and IF experiments were performed using o8G-specific antibodies. (G) Results of circKIAA1797 o8G RIP-qPCR in three groups of cells subjected to different treatments. (H) qPCR detection of circKIAA1797 expression after the treatment of cells with 2 mM NAC and 200 nM H2O2 for 0, 2 and 4 h. (I) Changes in the nuclear–cytoplasmic distribution of circKIAA1797 in A549 and H1299 cells were detected by a nuclear–cytoplasmic fractionation assay following H2O2 treatment. (J and K) Detection of circKIAA1797 binding to YBX1 by RIP-qPCR and agarose gel electrophoresis. (L) Results of CLIP-qPCR for the detection of circKIAA1797 binding to YBX1. (M) qPCR detection of circKIAA1797 expression after YBX1 was silenced. (N and O) After YBX1 was silenced, Act D experiments were conducted, and qPCR assays were performed to compare the half-life of circKIAA1797. (P) After YBX1 was silenced, a nuclear–cytoplasmic fractionation assay was conducted, and qPCR assays were performed to compare the changes in the nuclear–cytoplasmic distribution of circKIAA1797