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Image Search Results
Journal: Frontiers in Immunology
Article Title: Liquid-liquid phase separation-associated gene networks link EMT and ferroptosis to define a PDGFRB-centered prognostic signature in bladder cancer
doi: 10.3389/fimmu.2026.1846096
Figure Lengend Snippet: PDGFRB promotes proliferation, migration, and suppresses ferroptosis in bladder cancer cells. (A) In vitro droplet formation assay of purified recombinant EGFP-PDGFRB-IDR (residues 951–1089) at the indicated concentrations, imaged by confocal microscopy. Scale bar, 2 μm. (B) Western Blot analysis of PDGFRB protein levels in parental T24, shNC (scramble control), and shPDGFRB cells using anti-PDGFRB antibody, with β-actin as loading control. (C) Cell proliferation. CCK-8 assay showing cell viability of shNC and shPDGFRB T24 cells at indicated time points (0, 24, 48, 72, 96 h). (D) Cell migration. Left: Representative images of wound healing assay at 0 and 24 h. Scale bar, 500 μm. Right: Quantification of wound closure rate. (E) Mitochondrial morphology. Transmission electron microscopy images showing mitochondrial morphology in shNC and shPDGFRB T24 cells. Green arrows indicate normal mitochondria with intact cristae; red arrows indicate ferroptotic mitochondria with shrinkage and membrane densification. Scale bar, 0.5 μm. (F) Lipid peroxidation. Left: Ridge plot showing C11-BODIPY fluorescence intensity distribution in shNC and shPDGFRB T24 cells measured by flow cytometry. Right: Quantification of mean fluorescence intensity. (G) MDA levels. Malondialdehyde (MDA) levels in shNC and shPDGFRB T24 cells measured by MDA assay kit. (H) Ferroptosis rescue assay. CCK-8 assay showing cell viability of shNC and shPDGFRB T24 cells with or without Ferrostatin-1 (Fer-1, 2 μM) at indicated time points (0, 24, 48, 72, 96 h). All experiments were performed independently at least three times. For (C, D, F, G) , each independent experiment included two technical replicates (labeled shPDGFRB-1 and shPDGFRB-2) of the same shPDGFRB construct. Data are presented as mean ± s.d. For (B) , significance was calculated by one-way ANOVA. For (C, D, F, G) , significance was calculated by unpaired two-tailed Student's t test. For (H) , significance was calculated by two-way ANOVA. **p < 0.01, ***p < 0.001, ****p < 0.0001.
Article Snippet:
Techniques: Migration, In Vitro, Tube Formation Assay, Purification, Recombinant, Confocal Microscopy, Western Blot, Control, CCK-8 Assay, Wound Healing Assay, Transmission Assay, Electron Microscopy, Membrane, Fluorescence, Flow Cytometry, Multiple Displacement Amplification, Rescue Assay, Labeling, Construct, Two Tailed Test
Journal: Frontiers in Neurology
Article Title: Exosomal circ_0093708 as a potential ferroptosis biomarker in cerebral ischemia–reperfusion injury
doi: 10.3389/fneur.2025.1633393
Figure Lengend Snippet: Mining of key genes for ferroptosis and verification in external databases. (A) The 5-set Venn diagram showing the comprehensive strategy among suppressor ferroptosis-associated genes (green circle), unclassified ferroptosis-associated genes (orange circle), marker ferroptosis-associated genes (blue circle), driver ferroptosis-associated genes (pink circle), and differentially expressed genes (DEGs) (purple circle). (B) ROC analysis for DUSP1 in the discovery dataset. (C) ROC analysis for PTGS2 in the discovery dataset. (D) ROC analysis for DUSP1 in the validation dataset. (E) ROC analysis for PTGS2 in the validation dataset. ROC, receiver operating characteristic.
Article Snippet: We chose CIL56 (T4309,
Techniques: Marker, Biomarker Discovery
Journal: Frontiers in Neurology
Article Title: Exosomal circ_0093708 as a potential ferroptosis biomarker in cerebral ischemia–reperfusion injury
doi: 10.3389/fneur.2025.1633393
Figure Lengend Snippet: Inhibition of DUSP1 exacerbates ferroptosis in PC12 cells. (A) Cell viability after CIL56 treatment. (B) Intracellular MDA levels. (C) Effect of BCI on DUSP1 inhibition in the ferroptosis model. (D) Intracellular ROS levels (scale bar: 20 μm). (E) Protein expression of DUSP1, GPX4, and TFRC. (F) Quantification of GPX4 levels. (G) Quantification of TFRC levels. Data were analyzed by one-way ANOVA with Tukey’s post hoc test and presented as mean ± SD. Con, control.
Article Snippet: We chose CIL56 (T4309,
Techniques: Inhibition, Expressing, Control
Journal: Free radical biology & medicine
Article Title: Targeting SLC3A2 subunit of system X C - is essential for m 6 A reader YTHDC2 to be an endogenous ferroptosis inducer in lung adenocarcinoma.
doi: 10.1016/j.freeradbiomed.2021.03.023
Figure Lengend Snippet: Fig. 8. Schematic presentation of the study. Briefly, the m6A reader YTHDC2 is an endogenous ferroptosis inducer and its function is to suppress system XC −. In addition to what we’ve previously reported that the mRNA stability of SLC7A11 is suppressed by YTHDC2, in the present study we also found that SLC3A2, another subunit of system XC − can also be suppressed by YTHDC2 via targeting HOXA13-mediated transcription of SLC3A2, and the m6A methylation and subsequent destabilization of HOXA13 mRNA is a prerequisite for this process.
Article Snippet: Abbreviations YTHDC2 YT521-B homology containing 2 LUAD lung adenocarcinoma SLC7A11 solute carrier 7A11 OS overall survival IB immunoblotting RT-qPCR reverse transcription-quantitative PCR IHC immunohistochemistry ELISA enzyme-linked immunosorbent assay Dox Doxycycline ROS reactive oxygen species EMSA electrophoretic mobility shift assay ChIP chromatin immunoprecipitation RIP RNA immunoprecipitation PAR-CLIP photoactivatable ribonucleotide crosslinking and immunoprecipitation SLC3A2 solute carrier 3A2 HOXA13 Homeo box A13 3′UTR 3′ untranslated region GSH glutathione GPX4 glutathione peroxidase RSL3 RAS-selective
Techniques: Methylation