Oxidative damage can have a devastating effect on the structure and activity of proteins, and
may even lead to cell death. The sulfur-containing amino acids cysteine and methionine are …

Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin
superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in …

Genetically identical cells in the same stressful condition die at different times. The origin of
this stochasticity is unclear; it may arise from different initial conditions that affect the time of …

Exposure of cells to elevated levels of reactive oxygen species (ROS) damages DNA,
membrane lipids and proteins, which can potentially lead to cell death. In proteins, the sulfur …

The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in
all domains of life. With the discovery in the early 1990s that disulfide bond formation is …

The extensive use of copper-based fungicides in orchards, especially in vineyards, leads to
the accumulation of copper, which has caused growing concern. However, data on the …

Salmonella spp., one of the most common foodborne bacterial pathogens, has the ability to
survive under desiccation conditions in foods and food processing facilities for years. This …

Disulfide Bonds in Protein Folding and Stability | Oxidative Folding of Proteins: Basic
Principles, Cellular Regulation and Engineering | Books Gateway | Royal Society of Chemistry …

Diffusion within bacteria is often thought of as a “simple” random process by which
molecules collide and interact with each other. New research however shows that this is far …

Significance: Disturbance of glutathione (GSH) metabolism is a hallmark of numerous
diseases, yet GSH functions are poorly understood. One key to this question is to consider …