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Through a series of enzymatic reactions, a small protein molecule composed of 76 amino acid residues, ubiquitin, is attached to target proteins, ultimately leading to changes in the proteins localization and function or its degradation by the proteasome ( Figure 1 )

Although we have acquired knowledge about some toxic lipid states, including lipid membranes and lipid droplets of aberrant compositions, and peroxidated lipids (Figure 2), as well as about some toxic protein states, including misfolded oligomers (Figures 35), it is likely that additional toxic states will emerge, providing novel insights and mechanistic details of the connections between proteotoxicity and lipotoxicity

Recent data have commented on the CRP-binding capacity of lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1), which induces complement activation, leukocyte infiltration, and the modification of vascular response to vasodilators, mimicking a shared pathway for CRP and oxidized LDL in endothelial dysfunction

Our re-analysis of transcriptomic datasets of C