Unraveling Oxidative Stress Resistance: Molecular Properties Govern Proteome Vulnerability

Abstract

Oxidative stress alters cell viability, from microorganism irradiation sensitivity to human aging and neurodegeneration. Deleterious effects of protein carbonylation by reactive oxygen species 20

Large-scale genome sequencing reveals the driving forces of viruses in microalgal evolution

“…We also found that predicted enzymes in lysine biosynthesis pathways from the Kyoto encyclopedia of genes and genomes (KEGG) had higher counts, on average, in most saltwater species (Table S4; Data S10). Lysine was recently found to be important for oxidative stress resistance (Chang et al, 2020), and higher abundances of lysine in saltwater microalgal proteins might be necessary for their survival in the face of salt-induced oxidative stress.…”

Sustained-release nanocapsule based on a 3D COF for long-term enzyme prodrug therapy of cancer

“…Previous studies have confirmed that ROS can destroy the structure of proteins and further affect their properties. [9][10][11] As a type of protein, enzymes, such as HRP, will obviously lose their activity in the presence of ROS generated from IAA oxidation, which will further decrease the EPT efficiency. However, most of the reported studies did not pay attention to this feedback inhibition of HRP-IAA EPT.…”