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Figure 10: Model illustrating how quercetin protects cardiomyocytes from ROS treatment. ROS activates Src kinase and the overexpression of α-SNAP. ROS-induced α-SNAP causes phospho-Src-FAK complexes to move from the cytosol to a nearby inner cell membrane. ROS-activated p-Src and p-p38 stimulate the phosphorylation of STAT3 at tyrosine 705 and serine 727. After p-Src kinase and p-p38 activated STAT3, the p-STAT3 dimerized to translocate into nucleus. The dimerization of p-STAT3 induces the proinflammatory response gene expression (i.e., COX-2) in oxidative stress. Ena/VASP-like protein (Evl), which participates in actin binding and homologous recombination, is upregulated in ROS-induced cells and can repair ROS-damaged DNA. Elongation factor 1-alpha 1 (Eef1a1) decreased in oxidative stress resulting in cell death. Myosin regulatory light polypeptide 9 (Myl9), profilin-1 (Pfn1), and Eef1a1 are correlated with cytoskeleton, which may induce cell deadhesion and apoptosis. ROS inhibited the expression of isopentenyl-diphosphate delta-isomerase 1 (Idi1) in cells that may block the formation of lipophilic molecular such as sterols, ubiquinones, and terpenoids. Quercetin may protect ROS-damaged cardiomyocytes via these routes (stop sign in red). The proteins (red) were altered in a H2O2-dependant manner but reverted by pretreatment with quercetin.