Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

Disulfide bonds are important for the stability and function of many secreted proteins. In
Gram-negative bacteria, these linkages are catalyzed by thiol-disulfide oxidoreductases …

Antimicrobial resistance in Gram-negative bacteria is one of the greatest threats to global
health. New antibacterial strategies are urgently needed, and the development of antibiotic …

Antibiotic resistance has emerged as a serious threat to global public health in recent years.
Lack of novel antimicrobials, especially new classes of compounds, further aggravates the …

Recent years have witnessed a dramatic increase in bacterial antimicrobial resistance and a
decline in the development of novel antibiotics. New therapeutic strategies are urgently …

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

Aims: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in
bacteria. In pathogens, DsbA is a major facilitator of virulence constituting a target for …

Antibiotic-resistant and biofilm-associated infections constitute a rapidly growing issue. Use
of the last-resort antibiotic vancomycin is under threat due to the increasing appearance of …

The recent, rapid increase in bacterial antimicrobial resistance has become a major public
health concern. One approach to generate new classes of antibacterials is targeting …

Disulfide bond (Dsb) proteins, especially DsbA, represent a promising but as‐yet‐unrealized
target in combating multidrug‐resistant (MDR) bacteria because their precise subcellular …